PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 18773979-1 2008 Elongation factor Tu (EF-Tu), the protein responsible for delivering aminoacyl-tRNAs (aa-tRNAs) to ribosomal A site during translation, belongs to the group of guanosine-nucleotide (GTP/GDP) binding proteins. Guanosine Diphosphate 186-189 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 0-20 18773979-1 2008 Elongation factor Tu (EF-Tu), the protein responsible for delivering aminoacyl-tRNAs (aa-tRNAs) to ribosomal A site during translation, belongs to the group of guanosine-nucleotide (GTP/GDP) binding proteins. Guanosine Diphosphate 186-189 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 22-27 18773979-6 2008 In the second case, corresponding to the GTP hydrolysis by EF-Tu alone, the side chain of His85 stays away from the active site, and the chemical reaction GTP+H(2)O-->GDP+Pi proceeds without participation of the histidine but through water molecules. Guanosine Diphosphate 170-173 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 59-64 18562321-7 2008 Furthermore, the mutant forms show an 11-22-fold increase in rates of GDP dissociation from eEF1A compared with the wild type protein. Guanosine Diphosphate 70-73 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 92-97 17704259-5 2007 ZPR1 binds preferentially to GDP-bound eEF1A but does not directly influence the kinetics of nucleotide exchange or GTP hydrolysis. Guanosine Diphosphate 29-32 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 39-44 17397188-5 2007 Removal of Mg2+ from the EF-Tu x EF-Ts complex increased the rate constant of GDP release 2-fold, suggesting a small contribution to nucleotide exchange. Guanosine Diphosphate 78-81 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 25-30 16717093-5 2006 The effects are attributed to the interference of the mutations with the EF-Ts-induced movements of the P-loop of EF-Tu and changes at the domain 1/3 interface, leading to the release of the beta-phosphate group of GTP/GDP. Guanosine Diphosphate 219-222 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 114-119 16876786-2 2006 Kirromycin and enacyloxin block EF-Tu.GDP on the ribosome; pulvomycin and GE2270 A inhibit the interaction of EF-Tu.GTP with aa-tRNA. Guanosine Diphosphate 38-41 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 32-37 16876786-2 2006 Kirromycin and enacyloxin block EF-Tu.GDP on the ribosome; pulvomycin and GE2270 A inhibit the interaction of EF-Tu.GTP with aa-tRNA. Guanosine Diphosphate 38-41 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 110-115 17042495-3 2006 It was found that P(i) release from EF-Tu is >20-fold slower than GTP cleavage and limits the rate of the conformational switch of EF-Tu from the GTP- to the GDP-bound form. Guanosine Diphosphate 161-164 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 36-41 17042495-3 2006 It was found that P(i) release from EF-Tu is >20-fold slower than GTP cleavage and limits the rate of the conformational switch of EF-Tu from the GTP- to the GDP-bound form. Guanosine Diphosphate 161-164 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 134-139 16675455-2 2006 Stopped-flow kinetics using 2"-(or 3")-O-N-methylanthraniloyl (mant)-GDP showed spontaneous release of nucleotide from eEF1A is extremely slow and accelerated 700-fold by eEF1B alpha. Guanosine Diphosphate 69-72 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 119-124 15581367-6 2004 In contrast, the affinity for GDP is decreased 10-fold due to a marked increase in the dissociation rate of EF-Tu.GDP (25-fold) that mimics the action of EF-Ts, the GDP/GTP exchange factor of EF-Tu. Guanosine Diphosphate 30-33 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 108-113 15581367-6 2004 In contrast, the affinity for GDP is decreased 10-fold due to a marked increase in the dissociation rate of EF-Tu.GDP (25-fold) that mimics the action of EF-Ts, the GDP/GTP exchange factor of EF-Tu. Guanosine Diphosphate 30-33 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 192-197 15581367-6 2004 In contrast, the affinity for GDP is decreased 10-fold due to a marked increase in the dissociation rate of EF-Tu.GDP (25-fold) that mimics the action of EF-Ts, the GDP/GTP exchange factor of EF-Tu. Guanosine Diphosphate 114-117 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 108-113 15581367-6 2004 In contrast, the affinity for GDP is decreased 10-fold due to a marked increase in the dissociation rate of EF-Tu.GDP (25-fold) that mimics the action of EF-Ts, the GDP/GTP exchange factor of EF-Tu. Guanosine Diphosphate 114-117 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 192-197 11524957-3 2001 The concept of the shuttle role of elongation factor eEF1A is grounded; the factor, being in a GTP-bound form, delivers aminoacyl-tRNA to the ribosome and then, in the GDP form after hydrolysis of GTP on the ribosome, forms a complex with the deacylated tRNA and delivers it to the aminoacyl-tRNA synthetase. Guanosine Diphosphate 168-171 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 53-58 14623968-7 2003 Our results show that TCTP preferentially stabilized the GDP form of eEF1A, and, furthermore, impaired the GDP exchange reaction promoted by eEF1Bbeta. Guanosine Diphosphate 57-60 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 69-74 15317456-6 2004 In the GDP-bound form of eEF1A, this binding site exists only as two separate halves, which accounts for the much greater affinity of didemnins for the GTP-bound form of this elongation factor. Guanosine Diphosphate 7-10 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 25-30 12354112-0 2002 Novel complexes of mammalian translation elongation factor eEF1A.GDP with uncharged tRNA and aminoacyl-tRNA synthetase. Guanosine Diphosphate 65-68 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 59-64 12354112-18 2002 However, the addition of tRNAPhe accelerated eEF1A.GDP binding to the enzyme. Guanosine Diphosphate 51-54 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 45-50 12354112-19 2002 A possible role of these stable novel ternary and quaternary complexes of eEF1A.GDP with tRNA and ARS in the channeled elongation cycle is discussed. Guanosine Diphosphate 80-83 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 74-79 11045624-5 2000 Competition of GTP with a fluorescent derivative of GDP (mantGDP) for binding to EF-Tu(mt) was used to measure the dissociation constant of the EF-Tu(mt) x GTP complex (K(GTP) = 18 +/- 9 microM). Guanosine Diphosphate 52-55 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 81-90 11373622-1 2001 In the elongation cycle of protein biosynthesis, the nucleotide exchange factor eEF1Balpha catalyzes the exchange of GDP bound to the G-protein, eEF1A, for GTP. Guanosine Diphosphate 117-120 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 145-150 11373622-2 2001 To obtain more information about the recently solved eEF1A-eEF1Balpha structure, we determined the structures of the eEF1A-eEF1Balpha-GDP-Mg2+, eEF1A-eEF1Balpha-GDP and eEF1A-eEF1Balpha-GDPNP complexes at 3.0, 2.4 and 2.05 A resolution, respectively. Guanosine Diphosphate 134-137 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 53-58 11373622-2 2001 To obtain more information about the recently solved eEF1A-eEF1Balpha structure, we determined the structures of the eEF1A-eEF1Balpha-GDP-Mg2+, eEF1A-eEF1Balpha-GDP and eEF1A-eEF1Balpha-GDPNP complexes at 3.0, 2.4 and 2.05 A resolution, respectively. Guanosine Diphosphate 134-137 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 117-122 11373622-2 2001 To obtain more information about the recently solved eEF1A-eEF1Balpha structure, we determined the structures of the eEF1A-eEF1Balpha-GDP-Mg2+, eEF1A-eEF1Balpha-GDP and eEF1A-eEF1Balpha-GDPNP complexes at 3.0, 2.4 and 2.05 A resolution, respectively. Guanosine Diphosphate 134-137 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 117-122 11373622-2 2001 To obtain more information about the recently solved eEF1A-eEF1Balpha structure, we determined the structures of the eEF1A-eEF1Balpha-GDP-Mg2+, eEF1A-eEF1Balpha-GDP and eEF1A-eEF1Balpha-GDPNP complexes at 3.0, 2.4 and 2.05 A resolution, respectively. Guanosine Diphosphate 134-137 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 117-122 11373622-2 2001 To obtain more information about the recently solved eEF1A-eEF1Balpha structure, we determined the structures of the eEF1A-eEF1Balpha-GDP-Mg2+, eEF1A-eEF1Balpha-GDP and eEF1A-eEF1Balpha-GDPNP complexes at 3.0, 2.4 and 2.05 A resolution, respectively. Guanosine Diphosphate 161-164 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 53-58 11373622-2 2001 To obtain more information about the recently solved eEF1A-eEF1Balpha structure, we determined the structures of the eEF1A-eEF1Balpha-GDP-Mg2+, eEF1A-eEF1Balpha-GDP and eEF1A-eEF1Balpha-GDPNP complexes at 3.0, 2.4 and 2.05 A resolution, respectively. Guanosine Diphosphate 161-164 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 117-122 11373622-2 2001 To obtain more information about the recently solved eEF1A-eEF1Balpha structure, we determined the structures of the eEF1A-eEF1Balpha-GDP-Mg2+, eEF1A-eEF1Balpha-GDP and eEF1A-eEF1Balpha-GDPNP complexes at 3.0, 2.4 and 2.05 A resolution, respectively. Guanosine Diphosphate 161-164 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 117-122 11373622-2 2001 To obtain more information about the recently solved eEF1A-eEF1Balpha structure, we determined the structures of the eEF1A-eEF1Balpha-GDP-Mg2+, eEF1A-eEF1Balpha-GDP and eEF1A-eEF1Balpha-GDPNP complexes at 3.0, 2.4 and 2.05 A resolution, respectively. Guanosine Diphosphate 161-164 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 117-122 11045624-4 2000 Equilibrium dialysis with [3H]GDP was used to measure the equilibrium dissociation constant of the EF-Tu(mt) x GDP complex (K(GDP) = 1.0 +/- 0.1 microM). Guanosine Diphosphate 30-33 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 99-108 11045624-4 2000 Equilibrium dialysis with [3H]GDP was used to measure the equilibrium dissociation constant of the EF-Tu(mt) x GDP complex (K(GDP) = 1.0 +/- 0.1 microM). Guanosine Diphosphate 111-114 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 99-108 11045624-4 2000 Equilibrium dialysis with [3H]GDP was used to measure the equilibrium dissociation constant of the EF-Tu(mt) x GDP complex (K(GDP) = 1.0 +/- 0.1 microM). Guanosine Diphosphate 111-114 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 99-108 11045624-5 2000 Competition of GTP with a fluorescent derivative of GDP (mantGDP) for binding to EF-Tu(mt) was used to measure the dissociation constant of the EF-Tu(mt) x GTP complex (K(GTP) = 18 +/- 9 microM). Guanosine Diphosphate 52-55 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 144-153 11045624-7 2000 Both K(GDP) and K(GTP) for EF-Tu(mt) are quite different (about two orders of magnitude higher) than the dissociation constants of the corresponding complexes formed by Escherichia coli EF-Tu. Guanosine Diphosphate 7-10 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 27-36 11045624-7 2000 Both K(GDP) and K(GTP) for EF-Tu(mt) are quite different (about two orders of magnitude higher) than the dissociation constants of the corresponding complexes formed by Escherichia coli EF-Tu. Guanosine Diphosphate 7-10 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 27-32 11045624-8 2000 The forward and reverse rate constants for the association and dissociation of the EF-Tu(mt) x GDP complex were determined using the change in the fluorescence of mantGDP upon interaction with EF-Tu(mt). Guanosine Diphosphate 95-98 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 83-92 11045624-8 2000 The forward and reverse rate constants for the association and dissociation of the EF-Tu(mt) x GDP complex were determined using the change in the fluorescence of mantGDP upon interaction with EF-Tu(mt). Guanosine Diphosphate 95-98 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 193-202 11045624-9 2000 These values are in agreement with a simple equilibrium binding interaction between EF-Tu(mt) and GDP. Guanosine Diphosphate 98-101 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 84-93 11045624-10 2000 The results obtained are discussed in terms of the recently described crystal structure of the EF-Tu(mt) x GDP complex. Guanosine Diphosphate 107-110 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 95-104 9218959-3 1997 Structural studies of the complete functional cycle of EF-Tu reveal that it undergoes rather spectacular conformational changes when activated from the EF-Tu.GDP form to the EF-Tu.GTP form. Guanosine Diphosphate 158-161 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 55-60 9254632-6 1997 The small-angle X-ray scattering study described here was undertaken to ascertain if the form of EF-G that has high ribosome affinity, EF-G.GTP, the structure of which is unknown, could be a mimic of EF-Tu.GDP. Guanosine Diphosphate 206-209 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 200-205 10376675-5 1999 Elongation factor-G:GDP is now thought to leave the ribosome in a state ready for checking the codon-anticodon interaction of the aminoacyl-tRNA contained in the ternary complex of elongation factor-Tu. Guanosine Diphosphate 20-23 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 181-201 9254632-2 1997 Crystallographic investigations have revealed that EF-G.GDP resembles the EF-Tu.GTP. Guanosine Diphosphate 56-59 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 74-79 9254632-5 1997 However, its significance is uncertain because the affinity of EF-G.GDP for the ribosome is much lower than that of the ternary complex it resembles and because EF-Tu.GDP, the form of EF-Tu that has low ribosome affinity, has a conformation radically different from that of EF-Tu.GTP or EF-Tu in the ternary complex. Guanosine Diphosphate 68-71 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 184-189 9254632-5 1997 However, its significance is uncertain because the affinity of EF-G.GDP for the ribosome is much lower than that of the ternary complex it resembles and because EF-Tu.GDP, the form of EF-Tu that has low ribosome affinity, has a conformation radically different from that of EF-Tu.GTP or EF-Tu in the ternary complex. Guanosine Diphosphate 68-71 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 184-189 9254632-5 1997 However, its significance is uncertain because the affinity of EF-G.GDP for the ribosome is much lower than that of the ternary complex it resembles and because EF-Tu.GDP, the form of EF-Tu that has low ribosome affinity, has a conformation radically different from that of EF-Tu.GTP or EF-Tu in the ternary complex. Guanosine Diphosphate 68-71 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 184-189 9254632-5 1997 However, its significance is uncertain because the affinity of EF-G.GDP for the ribosome is much lower than that of the ternary complex it resembles and because EF-Tu.GDP, the form of EF-Tu that has low ribosome affinity, has a conformation radically different from that of EF-Tu.GTP or EF-Tu in the ternary complex. Guanosine Diphosphate 167-170 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 161-166 9254632-5 1997 However, its significance is uncertain because the affinity of EF-G.GDP for the ribosome is much lower than that of the ternary complex it resembles and because EF-Tu.GDP, the form of EF-Tu that has low ribosome affinity, has a conformation radically different from that of EF-Tu.GTP or EF-Tu in the ternary complex. Guanosine Diphosphate 167-170 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 184-189 9254632-5 1997 However, its significance is uncertain because the affinity of EF-G.GDP for the ribosome is much lower than that of the ternary complex it resembles and because EF-Tu.GDP, the form of EF-Tu that has low ribosome affinity, has a conformation radically different from that of EF-Tu.GTP or EF-Tu in the ternary complex. Guanosine Diphosphate 167-170 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 184-189 9254632-5 1997 However, its significance is uncertain because the affinity of EF-G.GDP for the ribosome is much lower than that of the ternary complex it resembles and because EF-Tu.GDP, the form of EF-Tu that has low ribosome affinity, has a conformation radically different from that of EF-Tu.GTP or EF-Tu in the ternary complex. Guanosine Diphosphate 167-170 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 184-189 9218959-3 1997 Structural studies of the complete functional cycle of EF-Tu reveal that it undergoes rather spectacular conformational changes when activated from the EF-Tu.GDP form to the EF-Tu.GTP form. Guanosine Diphosphate 158-161 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 152-157 9218959-3 1997 Structural studies of the complete functional cycle of EF-Tu reveal that it undergoes rather spectacular conformational changes when activated from the EF-Tu.GDP form to the EF-Tu.GTP form. Guanosine Diphosphate 158-161 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 152-157 7782317-1 1995 The elongation factor Tu (EF-Tu) is a member of the GTP/GDP-binding proteins and interacts with various partners during the elongation cycle of protein biosynthesis thereby mediating the correct binding of amino-acylated transfer RNA (aa-tRNA) to the acceptor site (A-site) of the ribosome. Guanosine Diphosphate 56-59 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 4-24 8665868-3 1996 In its presence, the migration velocity of both GTP- and GDP-bound EF-Tu on native PAGE is increased. Guanosine Diphosphate 57-60 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 67-72 8665868-4 1996 The stimulation of EF-Tu-GDP dissociation by EF-Ts is inhibited. Guanosine Diphosphate 25-28 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 19-24 8722020-4 1995 Elongation factor Tu (EF-Tu) undergoes a dramatic structural transition from its GDP-bound form to its active GTP-bound form, in which it binds aa-tRNA (aminoacyl-tRNA) in ternary complex. Guanosine Diphosphate 81-84 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 0-20 8722020-4 1995 Elongation factor Tu (EF-Tu) undergoes a dramatic structural transition from its GDP-bound form to its active GTP-bound form, in which it binds aa-tRNA (aminoacyl-tRNA) in ternary complex. Guanosine Diphosphate 81-84 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 22-27 8722020-5 1995 The effects of substitution mutations at three sites in domain I of EF-Tu, Gln124, Leu120, and Tyr160, all of which point into the domain I-domain III interface in both the GTP and GDP conformations of EF-Tu, were examined. Guanosine Diphosphate 181-184 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 68-73 8722020-5 1995 The effects of substitution mutations at three sites in domain I of EF-Tu, Gln124, Leu120, and Tyr160, all of which point into the domain I-domain III interface in both the GTP and GDP conformations of EF-Tu, were examined. Guanosine Diphosphate 181-184 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 202-207 7782317-1 1995 The elongation factor Tu (EF-Tu) is a member of the GTP/GDP-binding proteins and interacts with various partners during the elongation cycle of protein biosynthesis thereby mediating the correct binding of amino-acylated transfer RNA (aa-tRNA) to the acceptor site (A-site) of the ribosome. Guanosine Diphosphate 56-59 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 26-31 7782317-2 1995 After GTP hydrolysis EF-Tu is released in its GDP-bound state. Guanosine Diphosphate 46-49 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 21-26 7851417-1 1995 A fluorescent analogue of GDP, the 3"-O-anthraniloyl-GDP (anl-GDP) was demonstrated to bind to the elongation factor Tu (EF-Tu) with an affinity even higher than that of the parent nucleotide. Guanosine Diphosphate 26-29 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 99-119 7851417-1 1995 A fluorescent analogue of GDP, the 3"-O-anthraniloyl-GDP (anl-GDP) was demonstrated to bind to the elongation factor Tu (EF-Tu) with an affinity even higher than that of the parent nucleotide. Guanosine Diphosphate 26-29 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 121-126 7851417-4 1995 In this way, it was also easily proven that, in the presence of aurodox (N-methylkirromycin), an antibiotic impairing EF-Tu biological function, the exchange kinetics between the protein-bound labeled GDP and the natural nucleotide was faster. Guanosine Diphosphate 201-204 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 118-123 2110000-2 1990 The effects of GDP and of aurodox (N-methylkirromycin) on the affinity of elongation factor Tu (EF-Tu) for aminoacyl-tRNA (aa-tRNA) have been quantified spectroscopically by using Phe-tRNA(Phe)-Fl8, a functionally active analogue of Phe-tRNA(Phe) with a fluorescein dye convalently attached to the s4U-8 base. Guanosine Diphosphate 15-18 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 74-94 8462668-3 1993 Based on the similarities of ras-p21 and elongation factor Tu we propose here a model of the GDP state of ras-p21 that is in agreement with all relevant experimental evidence. Guanosine Diphosphate 93-96 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 41-61 1740128-4 1992 Specific differences between p21 and EF-Tu were found in the action of divalent anions which strongly enhance the dissociation rate of p21.GDP without affecting that of EF-Tu. Guanosine Diphosphate 139-142 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 37-42 1663155-12 1991 For the docking of the guanine derivative, the X-ray structure of Elongation Factor Tu (EF-Tu), co-crystallized with guanosine diphosphate, was taken as reference. Guanosine Diphosphate 117-138 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 66-86 1663155-12 1991 For the docking of the guanine derivative, the X-ray structure of Elongation Factor Tu (EF-Tu), co-crystallized with guanosine diphosphate, was taken as reference. Guanosine Diphosphate 117-138 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 88-93 2119812-1 1990 Mutagenesis was carried out in the N-terminal domain of elongation factor Tu (EF-Tu) to characterize the structure-function relationships of this model GTP binding protein with respect to stability, the interaction with GTP and GDP, and the catalytic activity. Guanosine Diphosphate 228-231 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 56-76 1740128-6 1992 The concentrations of Mg2+ influencing the dissociation rate of the p21.GDP complex are much higher than for the intrinsic GTPase activity, an effect also observed for EF-Tu. Guanosine Diphosphate 72-75 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 168-173 2110000-2 1990 The effects of GDP and of aurodox (N-methylkirromycin) on the affinity of elongation factor Tu (EF-Tu) for aminoacyl-tRNA (aa-tRNA) have been quantified spectroscopically by using Phe-tRNA(Phe)-Fl8, a functionally active analogue of Phe-tRNA(Phe) with a fluorescein dye convalently attached to the s4U-8 base. Guanosine Diphosphate 15-18 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 96-101 2110000-3 1990 The association of EF-Tu.GDP with Phe-tRNA(Phe)-Fl8 resulted in an average increase of 33% in fluorescein emission intensity. Guanosine Diphosphate 25-28 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 19-24 2110000-4 1990 This spectral change was used to monitor the extent of ternary complex formation as a function of EF-Tu.GDP concentration, and hence to obtain a dissociation constant, directly and at equilibrium, for the EF-Tu.GDP-containing ternary complex. Guanosine Diphosphate 104-107 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 98-103 2110000-4 1990 This spectral change was used to monitor the extent of ternary complex formation as a function of EF-Tu.GDP concentration, and hence to obtain a dissociation constant, directly and at equilibrium, for the EF-Tu.GDP-containing ternary complex. Guanosine Diphosphate 104-107 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 205-210 2110000-4 1990 This spectral change was used to monitor the extent of ternary complex formation as a function of EF-Tu.GDP concentration, and hence to obtain a dissociation constant, directly and at equilibrium, for the EF-Tu.GDP-containing ternary complex. Guanosine Diphosphate 211-214 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 98-103 2110000-4 1990 This spectral change was used to monitor the extent of ternary complex formation as a function of EF-Tu.GDP concentration, and hence to obtain a dissociation constant, directly and at equilibrium, for the EF-Tu.GDP-containing ternary complex. Guanosine Diphosphate 211-214 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 205-210 2110000-5 1990 The Kd for the Phe-tRNA(Phe)-Fl8.EF-Tu.GDP complex was found to average 28.5 microM, more than 33,000-fold greater than the Kd of the Phe-tRNA(Phe)-Fl8.EF-Tu.GTP complex under the same conditions. Guanosine Diphosphate 39-42 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 33-38 2110000-5 1990 The Kd for the Phe-tRNA(Phe)-Fl8.EF-Tu.GDP complex was found to average 28.5 microM, more than 33,000-fold greater than the Kd of the Phe-tRNA(Phe)-Fl8.EF-Tu.GTP complex under the same conditions. Guanosine Diphosphate 39-42 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 152-157 2110000-7 1990 Thus, the hydrolysis of the ternary complex GTP results in a dramatic decrease in the affinity of EF-Tu for aa-tRNA, thereby facilitating the release of EF-Tu.GDP from the aa-tRNA on the ribosome. Guanosine Diphosphate 159-162 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 98-103 2110000-7 1990 Thus, the hydrolysis of the ternary complex GTP results in a dramatic decrease in the affinity of EF-Tu for aa-tRNA, thereby facilitating the release of EF-Tu.GDP from the aa-tRNA on the ribosome. Guanosine Diphosphate 159-162 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 153-158 2110000-9 1990 The binding of aurodox to EF-Tu therefore both considerably strengthens EF-Tu.GDP affinity for aa-tRNA and also weakens EF-Tu.GTP affinity for aa-tRNA. Guanosine Diphosphate 78-81 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 26-31 2110000-9 1990 The binding of aurodox to EF-Tu therefore both considerably strengthens EF-Tu.GDP affinity for aa-tRNA and also weakens EF-Tu.GTP affinity for aa-tRNA. Guanosine Diphosphate 78-81 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 72-77 2110000-9 1990 The binding of aurodox to EF-Tu therefore both considerably strengthens EF-Tu.GDP affinity for aa-tRNA and also weakens EF-Tu.GTP affinity for aa-tRNA. Guanosine Diphosphate 78-81 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 72-77 3350808-1 1988 The release of a chromophoric analogue of GDP, 2-amino-6-mercaptopurine riboside 5"-diphosphate (thioGDP), from its complex with elongation factor Tu (EF-Tu) is catalyzed by elongation factor Ts (EF-Ts). Guanosine Diphosphate 42-45 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 129-149 2508560-0 1989 Site-directed mutagenesis of the GDP binding domain of bacterial elongation factor Tu. Guanosine Diphosphate 33-36 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 65-85 2508560-8 1989 This mutation is theoretically equivalent to reversion of the Gly to Val transforming mutation of the cellular form of the ras gene product p21, a protein proposed to be structurally similar to EF-Tu in the GDP binding domain. Guanosine Diphosphate 207-210 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 194-199 2510820-9 1989 These results strongly support the hypothesis that aurodox not only confers a "GTP-like" conformation to the EF-Tu.GDP complex but also produces a less stable folding of the protein around the tryptophan residue that may contribute to the multiple functional effects of this antibiotic. Guanosine Diphosphate 115-118 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 109-114 3181143-1 1988 Val20 of elongation factor Tu (EF-Tu), one of the best-characterized GTP binding proteins, is a variable residue within the consensus motif G-X-X-X-X-G-K involved in the interaction with the phosphates of GDP/GTP. Guanosine Diphosphate 205-208 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 9-29 3181143-1 1988 Val20 of elongation factor Tu (EF-Tu), one of the best-characterized GTP binding proteins, is a variable residue within the consensus motif G-X-X-X-X-G-K involved in the interaction with the phosphates of GDP/GTP. Guanosine Diphosphate 205-208 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 31-36 3181143-7 1988 As in p21, this position in EF-Tu is critical, influencing specifically the GDP/GTP interaction as well as other functions. Guanosine Diphosphate 76-79 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 28-33 3350808-1 1988 The release of a chromophoric analogue of GDP, 2-amino-6-mercaptopurine riboside 5"-diphosphate (thioGDP), from its complex with elongation factor Tu (EF-Tu) is catalyzed by elongation factor Ts (EF-Ts). Guanosine Diphosphate 42-45 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 151-156 6377304-4 1984 In the case of elongation factor Tu X GDP X kirromycin, cross-linking was found at lysine-208; in elongation factor Tu X GTP X kirromycin, cross-linking was at lysine-208 and lysine-237. Guanosine Diphosphate 38-41 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 15-35 3297141-5 1987 Compared with wild-type EF-Tu, EF-TuBo displays essentially the same affinity for GDP and GTP, with only the dissociation rate of EF-Tu GTP being slightly faster. Guanosine Diphosphate 82-85 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 31-36 3514605-4 1986 These are the rate constant for GTP hydrolysis, which plays an important role in the fidelity of ternary complex selection by the ribosome, and the rate constant for EF-Tu.GDP dissociation from the ribosome, which plays an equally important role in subsequent proofreading of the aa-tRNA. Guanosine Diphosphate 172-175 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 166-171 3514605-6 1986 These interactions determine the absolute value of the rate constants for GTP hydrolysis and EF-Tu.GDP dissociation. Guanosine Diphosphate 99-102 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 93-98 3276311-3 1988 From sequence homology with the bacterial elongation factor Tu (EF-Tu) and the known X-ray structure of the EF-Tu.GDP.Mg2+ complex it may be inferred that the Phe residue in question is either Phe78 or Phe82 in the p21 sequence. Guanosine Diphosphate 114-117 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 42-62 3276311-3 1988 From sequence homology with the bacterial elongation factor Tu (EF-Tu) and the known X-ray structure of the EF-Tu.GDP.Mg2+ complex it may be inferred that the Phe residue in question is either Phe78 or Phe82 in the p21 sequence. Guanosine Diphosphate 114-117 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 64-69 3276311-3 1988 From sequence homology with the bacterial elongation factor Tu (EF-Tu) and the known X-ray structure of the EF-Tu.GDP.Mg2+ complex it may be inferred that the Phe residue in question is either Phe78 or Phe82 in the p21 sequence. Guanosine Diphosphate 114-117 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 108-113 3651421-0 1987 Intrinsic fluorescence of elongation factor Tu in its complexes with GDP and elongation factor Ts. Guanosine Diphosphate 69-72 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 26-46 3651421-1 1987 The intrinsic fluorescence properties of elongation factor Tu (EF-Tu) in its complexes with GDP and elongation factor Ts (EF-Ts) have been investigated. Guanosine Diphosphate 92-95 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 41-61 3651421-1 1987 The intrinsic fluorescence properties of elongation factor Tu (EF-Tu) in its complexes with GDP and elongation factor Ts (EF-Ts) have been investigated. Guanosine Diphosphate 92-95 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 63-68 3651421-7 1987 Steady-state and dynamic polarization measurements revealed limited local mobility for the tryptophan in the EF-Tu x GDP complex whereas formation of the EF-Tu x EF-Ts complex led to a dramatic increase in this local mobility. Guanosine Diphosphate 117-120 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 109-114 366156-0 1978 High resolution x-ray crystallographic analysis of a modified form of the elongation factor Tu: guanosine diphosphate complex. Guanosine Diphosphate 96-117 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 74-94 16453409-2 1982 The EF-Ts catalyzed release of GDP from EF-Tu was measured independently in a nucleotide exchange assay. Guanosine Diphosphate 31-34 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 40-45 16453409-3 1982 We conclude that the rate-limiting step for the EF-Tu cycle in protein synthesis in the absence of EF-Ts is the release of GDP. Guanosine Diphosphate 123-126 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 48-53 6323160-3 1984 These replacements substantially lower the affinity of EF-Tu.GDP for the antibiotic kirromycin. Guanosine Diphosphate 61-64 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 55-60 6323160-11 1984 In the presence of kirromycin this mutant species of EF-Tu.GDP does not bind to the ribosome, in contrast to its wild-type counterpart. Guanosine Diphosphate 59-62 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 53-58 6953412-5 1982 The eIF-2 and GDP exchanges are compatible with the reaction eIF-2-GDP + SP in equilibrium EIF-2-SP + GDP reminiscent of the exchange between the Tu and Ts components of prokaryotic elongation factor 1 (EF-Tu and EF-Ts, respectively) EF-Tu-GDP + EF-Ts in equilibrium EF-Tu-EF-Ts + GDP. Guanosine Diphosphate 14-17 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 203-208 6953412-5 1982 The eIF-2 and GDP exchanges are compatible with the reaction eIF-2-GDP + SP in equilibrium EIF-2-SP + GDP reminiscent of the exchange between the Tu and Ts components of prokaryotic elongation factor 1 (EF-Tu and EF-Ts, respectively) EF-Tu-GDP + EF-Ts in equilibrium EF-Tu-EF-Ts + GDP. Guanosine Diphosphate 14-17 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 234-239 6953412-5 1982 The eIF-2 and GDP exchanges are compatible with the reaction eIF-2-GDP + SP in equilibrium EIF-2-SP + GDP reminiscent of the exchange between the Tu and Ts components of prokaryotic elongation factor 1 (EF-Tu and EF-Ts, respectively) EF-Tu-GDP + EF-Ts in equilibrium EF-Tu-EF-Ts + GDP. Guanosine Diphosphate 14-17 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 234-239 6953412-5 1982 The eIF-2 and GDP exchanges are compatible with the reaction eIF-2-GDP + SP in equilibrium EIF-2-SP + GDP reminiscent of the exchange between the Tu and Ts components of prokaryotic elongation factor 1 (EF-Tu and EF-Ts, respectively) EF-Tu-GDP + EF-Ts in equilibrium EF-Tu-EF-Ts + GDP. Guanosine Diphosphate 67-70 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 203-208 6953412-5 1982 The eIF-2 and GDP exchanges are compatible with the reaction eIF-2-GDP + SP in equilibrium EIF-2-SP + GDP reminiscent of the exchange between the Tu and Ts components of prokaryotic elongation factor 1 (EF-Tu and EF-Ts, respectively) EF-Tu-GDP + EF-Ts in equilibrium EF-Tu-EF-Ts + GDP. Guanosine Diphosphate 67-70 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 234-239 6953412-5 1982 The eIF-2 and GDP exchanges are compatible with the reaction eIF-2-GDP + SP in equilibrium EIF-2-SP + GDP reminiscent of the exchange between the Tu and Ts components of prokaryotic elongation factor 1 (EF-Tu and EF-Ts, respectively) EF-Tu-GDP + EF-Ts in equilibrium EF-Tu-EF-Ts + GDP. Guanosine Diphosphate 67-70 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 234-239 6953412-5 1982 The eIF-2 and GDP exchanges are compatible with the reaction eIF-2-GDP + SP in equilibrium EIF-2-SP + GDP reminiscent of the exchange between the Tu and Ts components of prokaryotic elongation factor 1 (EF-Tu and EF-Ts, respectively) EF-Tu-GDP + EF-Ts in equilibrium EF-Tu-EF-Ts + GDP. Guanosine Diphosphate 67-70 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 203-208 6953412-5 1982 The eIF-2 and GDP exchanges are compatible with the reaction eIF-2-GDP + SP in equilibrium EIF-2-SP + GDP reminiscent of the exchange between the Tu and Ts components of prokaryotic elongation factor 1 (EF-Tu and EF-Ts, respectively) EF-Tu-GDP + EF-Ts in equilibrium EF-Tu-EF-Ts + GDP. Guanosine Diphosphate 67-70 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 234-239 6953412-5 1982 The eIF-2 and GDP exchanges are compatible with the reaction eIF-2-GDP + SP in equilibrium EIF-2-SP + GDP reminiscent of the exchange between the Tu and Ts components of prokaryotic elongation factor 1 (EF-Tu and EF-Ts, respectively) EF-Tu-GDP + EF-Ts in equilibrium EF-Tu-EF-Ts + GDP. Guanosine Diphosphate 67-70 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 234-239 6953412-5 1982 The eIF-2 and GDP exchanges are compatible with the reaction eIF-2-GDP + SP in equilibrium EIF-2-SP + GDP reminiscent of the exchange between the Tu and Ts components of prokaryotic elongation factor 1 (EF-Tu and EF-Ts, respectively) EF-Tu-GDP + EF-Ts in equilibrium EF-Tu-EF-Ts + GDP. Guanosine Diphosphate 67-70 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 203-208 6953412-5 1982 The eIF-2 and GDP exchanges are compatible with the reaction eIF-2-GDP + SP in equilibrium EIF-2-SP + GDP reminiscent of the exchange between the Tu and Ts components of prokaryotic elongation factor 1 (EF-Tu and EF-Ts, respectively) EF-Tu-GDP + EF-Ts in equilibrium EF-Tu-EF-Ts + GDP. Guanosine Diphosphate 67-70 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 234-239 6953412-5 1982 The eIF-2 and GDP exchanges are compatible with the reaction eIF-2-GDP + SP in equilibrium EIF-2-SP + GDP reminiscent of the exchange between the Tu and Ts components of prokaryotic elongation factor 1 (EF-Tu and EF-Ts, respectively) EF-Tu-GDP + EF-Ts in equilibrium EF-Tu-EF-Ts + GDP. Guanosine Diphosphate 67-70 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 234-239 6765192-6 1982 These data strongly suggest that kirromycin induces in EF-Tu.GDP an additional tRNA binding site that can bind uncharged tRNA, aminoacyl-tRNA, and N- acetylaminoacyl -tRNA. Guanosine Diphosphate 61-64 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 55-60 6765192-3 1982 Binding of aminoacyl-tRNA added at increasing concentrations to a solution of 40 microM EF-Tu.GDP.kirromycin complex re-exposes the TPCK target site on the protein. Guanosine Diphosphate 94-97 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 88-93 6765192-7 1982 Support for this assumption is provided by measuring the modification of EF-Tu.GDP with the sulfhydryl reagent NEM. Guanosine Diphosphate 79-82 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 73-78 6765192-9 1982 Mapping of the tryptic peptides of EF-Tu.GDP labeled with [14C]TPCK revealed only one target site for this agent, i.e., cysteine-81. Guanosine Diphosphate 41-44 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 35-40 364475-1 1978 Pulvomycin and the synonymous antibiotics labilomycin and 1063-Z are shown to inhibit prokaryotic protein synthesis by acting on elongation factor Tu (EF-Tu): in the presence of the antibiotic, the affinity of EF-Tu for guanine nucleotides is altered, the EF-Tu.GDP/GTP exchange is catalyzed, and the formation of the EF-Tu.GTP complex is stimulated. Guanosine Diphosphate 262-265 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 129-149 364475-1 1978 Pulvomycin and the synonymous antibiotics labilomycin and 1063-Z are shown to inhibit prokaryotic protein synthesis by acting on elongation factor Tu (EF-Tu): in the presence of the antibiotic, the affinity of EF-Tu for guanine nucleotides is altered, the EF-Tu.GDP/GTP exchange is catalyzed, and the formation of the EF-Tu.GTP complex is stimulated. Guanosine Diphosphate 262-265 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 151-156 364475-1 1978 Pulvomycin and the synonymous antibiotics labilomycin and 1063-Z are shown to inhibit prokaryotic protein synthesis by acting on elongation factor Tu (EF-Tu): in the presence of the antibiotic, the affinity of EF-Tu for guanine nucleotides is altered, the EF-Tu.GDP/GTP exchange is catalyzed, and the formation of the EF-Tu.GTP complex is stimulated. Guanosine Diphosphate 262-265 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 210-215 364475-1 1978 Pulvomycin and the synonymous antibiotics labilomycin and 1063-Z are shown to inhibit prokaryotic protein synthesis by acting on elongation factor Tu (EF-Tu): in the presence of the antibiotic, the affinity of EF-Tu for guanine nucleotides is altered, the EF-Tu.GDP/GTP exchange is catalyzed, and the formation of the EF-Tu.GTP complex is stimulated. Guanosine Diphosphate 262-265 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 210-215 364475-1 1978 Pulvomycin and the synonymous antibiotics labilomycin and 1063-Z are shown to inhibit prokaryotic protein synthesis by acting on elongation factor Tu (EF-Tu): in the presence of the antibiotic, the affinity of EF-Tu for guanine nucleotides is altered, the EF-Tu.GDP/GTP exchange is catalyzed, and the formation of the EF-Tu.GTP complex is stimulated. Guanosine Diphosphate 262-265 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 210-215 1099087-3 1975 The conformational difference between polypeptide chain elongation factor Tu (EF-Tu)-GTP and EF-Tu-GDP has been studied using hydrophobic and fluorescent probes. Guanosine Diphosphate 99-102 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 93-98 323049-0 1977 Structural requirements of the GDP binding site of elongation factor Tu. Guanosine Diphosphate 31-34 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 51-71 15625861-2 1976 The EF-Tu synthesized was identified by its immunological properties, gel analysis, and its ability to interact with GDP and EF-Ts. Guanosine Diphosphate 117-120 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 4-9 187578-3 1976 The conformational transitions of polypeptide chain elongation factor Tu (EF-Tu) associated with the ligand change from GDP to GTP and also with the displacement of GDP by elongation factor Ts (EF-Ts) have been investigated using the spin-labeling technique. Guanosine Diphosphate 120-123 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 52-72 187578-3 1976 The conformational transitions of polypeptide chain elongation factor Tu (EF-Tu) associated with the ligand change from GDP to GTP and also with the displacement of GDP by elongation factor Ts (EF-Ts) have been investigated using the spin-labeling technique. Guanosine Diphosphate 120-123 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 74-79 187578-3 1976 The conformational transitions of polypeptide chain elongation factor Tu (EF-Tu) associated with the ligand change from GDP to GTP and also with the displacement of GDP by elongation factor Ts (EF-Ts) have been investigated using the spin-labeling technique. Guanosine Diphosphate 165-168 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 52-72 187578-3 1976 The conformational transitions of polypeptide chain elongation factor Tu (EF-Tu) associated with the ligand change from GDP to GTP and also with the displacement of GDP by elongation factor Ts (EF-Ts) have been investigated using the spin-labeling technique. Guanosine Diphosphate 165-168 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 74-79 187578-5 1976 The electron spin resonance (ESR) spectra of EF-Tu-GDP labeled with these reagents generally consisted of two components, one narrow and one broad, corresponding to labels relatively weakly and strongly immobilized, respectively. Guanosine Diphosphate 51-54 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 45-50 187578-7 1976 The spectra of spin-labeled EF-Tu-GDP changed markedly when its GDP moiety was replaced by GTP through incubation with phosphoenolpyruvate and pyruvate kinase [EC 2.7.1.40], the broad component increasing at the expense of the narrow component. Guanosine Diphosphate 34-37 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 28-33 187578-7 1976 The spectra of spin-labeled EF-Tu-GDP changed markedly when its GDP moiety was replaced by GTP through incubation with phosphoenolpyruvate and pyruvate kinase [EC 2.7.1.40], the broad component increasing at the expense of the narrow component. Guanosine Diphosphate 64-67 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 28-33 187578-9 1976 The GTP-induced spectral change was reversed upon conversion of labeled EF-Tu-GTP to EF-Tu-GDP by addition of excess GDP. Guanosine Diphosphate 91-94 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 72-77 187578-9 1976 The GTP-induced spectral change was reversed upon conversion of labeled EF-Tu-GTP to EF-Tu-GDP by addition of excess GDP. Guanosine Diphosphate 91-94 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 85-90 187578-10 1976 A similar type of spectral change was also observed when spin-labeled EF-Tu-GDP was incubated with EF-Ts to form labeled EF-Tu-EF-Ts complex. Guanosine Diphosphate 76-79 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 70-75 187578-10 1976 A similar type of spectral change was also observed when spin-labeled EF-Tu-GDP was incubated with EF-Ts to form labeled EF-Tu-EF-Ts complex. Guanosine Diphosphate 76-79 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 121-126 1097432-6 1975 However, when EF-Tu and Gpp(CH2)p bound to the ribosomal complex were released by centrifugation through 10% sucrose containing 0.2 mM GDP, the yield of the dipeptide was correspondingly increased. Guanosine Diphosphate 135-138 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 14-19 1097432-8 1975 The subsequent conversion of EF-Tu.GTP to EF-Tu.GDP, a form of EF-Tu with low affinity for ribosomes as well as for Phe-tRNA, resulted in the detachment of EF-Tu. Guanosine Diphosphate 48-51 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 29-34 1097432-8 1975 The subsequent conversion of EF-Tu.GTP to EF-Tu.GDP, a form of EF-Tu with low affinity for ribosomes as well as for Phe-tRNA, resulted in the detachment of EF-Tu. Guanosine Diphosphate 48-51 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 42-47 1097432-8 1975 The subsequent conversion of EF-Tu.GTP to EF-Tu.GDP, a form of EF-Tu with low affinity for ribosomes as well as for Phe-tRNA, resulted in the detachment of EF-Tu. Guanosine Diphosphate 48-51 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 42-47 1097432-8 1975 The subsequent conversion of EF-Tu.GTP to EF-Tu.GDP, a form of EF-Tu with low affinity for ribosomes as well as for Phe-tRNA, resulted in the detachment of EF-Tu. Guanosine Diphosphate 48-51 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 42-47 4741543-0 1973 Evidence for conformational changes in elongation factor Tu induced by GTP and GDP. Guanosine Diphosphate 79-82 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 39-59 1099087-6 1975 The conformational change was found to be reversible and the spectrum promptly returned to that of EF-Tu-GDP-ANS complex upon addition of excess GDP. Guanosine Diphosphate 105-108 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 99-104 1099087-10 1975 Another reagent, N-(1-anilinonaphthyl-4) maleimide (ANM) was covalently bound to the sulfhydryl group in EF-Tu-GDP which is essential for interaction with aminoacyl-tRNA. Guanosine Diphosphate 111-114 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 105-110 1099087-12 1975 Measurements of the kinetics of the binding revealed that ANM reacted rapidly with the sulfhydryl group in EF-Tu-GTP, while the reaction with that in EF-Tu-GDP proceeded more sluggishly. Guanosine Diphosphate 156-159 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 150-155 1099087-13 1975 The difference in the reactivity of the sulfhydryl group essential for aminoacyl-tRNA binding between EF-Tu-GTP and EF-Tu-GDP probably reflects a conformational transition of the protein near the active site. Guanosine Diphosphate 122-125 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 116-121 1099087-16 1975 249, 3311), demonstrate that reversible conformational transition does occur in EF-Tu on changing the ligand from GDP to GTP. Guanosine Diphosphate 114-117 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 80-85 31058500-4 2019 EF-Tu alternates between GTP- and GDP-bound conformations during its functional cycle, representing the "on" and "off" states, respectively. Guanosine Diphosphate 34-37 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 0-5 31058500-6 2019 Additionally, molecular dynamics (MD) simulations indicate that enthalpic stabilization of GDP binding compared to GTP binding originates in the backbone hydrogen bonding network of EF-Tu. Guanosine Diphosphate 91-94 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 182-187 31058500-7 2019 In contrast, binding of GTP to EF-Tu is entropically driven by the liberation of bound water during the GDP- to GTP-bound transition. Guanosine Diphosphate 104-107 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 31-36 31058500-8 2019 GDP binding to the apo conformation of EF-Tu is both enthalpically and entropically favored, a feature unique among translational GTPases. Guanosine Diphosphate 0-3 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 39-44 25326326-1 2014 Eukaryotic elongation factor eEF1A transits between the GTP- and GDP-bound conformations during the ribosomal polypeptide chain elongation. Guanosine Diphosphate 65-68 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 29-34 26073967-7 2015 We have determined the crystal structures of the following reaction intermediates: two structures of EF-Tu:GDP:EF-Ts (2.2 and 1.8A resolution), EF-Tu:PO4:EF-Ts (1.9A resolution), EF-Tu:GDPNP:EF-Ts (2.2A resolution) and EF-Tu:GDPNP:pulvomycin:Mg(2+):EF-Ts (3.5A resolution). Guanosine Diphosphate 107-110 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 101-106 29417736-4 2018 We hypothesize that the exit rate of eukaryotic translation elongation factor 1A (eEF1A)*GDP from the 80S ribosome depends on the protein affinity to specific aminoacyl-tRNA remaining on the ribosome after GTP hydrolysis. Guanosine Diphosphate 89-92 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 37-80 29417736-4 2018 We hypothesize that the exit rate of eukaryotic translation elongation factor 1A (eEF1A)*GDP from the 80S ribosome depends on the protein affinity to specific aminoacyl-tRNA remaining on the ribosome after GTP hydrolysis. Guanosine Diphosphate 89-92 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 82-87 29417736-5 2018 Subsequently, a slower dissociation of eEF1A*GDP from certain aminoacyl-tRNAs in the ribosome can negatively influence the ribosomal elongation rate in a tRNA-dependent and mRNA-independent way. Guanosine Diphosphate 45-48 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 39-44 29417736-6 2018 The specific tRNA-dependent departure rate of eEF1A*GDP from the ribosome is suggested to be a novel factor contributing to the overall translation elongation control in eukaryotic cells. Guanosine Diphosphate 52-55 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 46-51 27837019-3 2016 First, aa-tRNAs in ternary complex with EF-Tu GDP are selected in a step where the accuracy increases linearly with increasing aa-tRNA affinity to EF-Tu. Guanosine Diphosphate 46-49 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 40-45 27837019-3 2016 First, aa-tRNAs in ternary complex with EF-Tu GDP are selected in a step where the accuracy increases linearly with increasing aa-tRNA affinity to EF-Tu. Guanosine Diphosphate 46-49 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 147-152 27837019-4 2016 Then, following dissociation of EF-Tu GDP from the ribosome, the accuracy is further increased in a second and apparently EF-Tu-independent step. Guanosine Diphosphate 38-41 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 32-37 27837019-4 2016 Then, following dissociation of EF-Tu GDP from the ribosome, the accuracy is further increased in a second and apparently EF-Tu-independent step. Guanosine Diphosphate 38-41 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 122-127 25326326-3 2014 Correct codon-anticodon recognition triggers GTP hydrolysis, with subsequent dissociation of eEF1A*GDP from the ribosome. Guanosine Diphosphate 99-102 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 93-98 25326326-6 2014 Here, we report the first crystal structure of the mammalian eEF1A2*GDP complex which indicates major differences in the organization of the nucleotide-binding domain and intramolecular movements of eEF1A compared to EF-Tu. Guanosine Diphosphate 68-71 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 61-66 25326326-6 2014 Here, we report the first crystal structure of the mammalian eEF1A2*GDP complex which indicates major differences in the organization of the nucleotide-binding domain and intramolecular movements of eEF1A compared to EF-Tu. Guanosine Diphosphate 68-71 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 217-222 25326326-7 2014 Our results explain the nucleotide exchange mechanism in the mammalian eEF1A and suggest that the first step of eEF1A*GDP dissociation from the 80S ribosome is the rotation of the nucleotide-binding domain observed after GTP hydrolysis. Guanosine Diphosphate 118-121 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 71-76 25326326-7 2014 Our results explain the nucleotide exchange mechanism in the mammalian eEF1A and suggest that the first step of eEF1A*GDP dissociation from the 80S ribosome is the rotation of the nucleotide-binding domain observed after GTP hydrolysis. Guanosine Diphosphate 118-121 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 112-117 24079513-4 2013 The unnatural amino acid appears to disrupt the interactions that balance the strength of tRNA binding to EF-Tu-GTP with the velocity of tRNA dissociation from EF-Tu-GDP on the ribosome, which ensure uniform incorporation of standard amino acids. Guanosine Diphosphate 166-169 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 106-111 22740700-2 2012 By analogy to elongation factor Tu (EF-Tu), SelB is expected to control the delivery and release of Sec-tRNA(Sec) to the ribosome by the structural switch between GTP- and GDP-bound conformations. Guanosine Diphosphate 172-175 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 14-34 22740700-2 2012 By analogy to elongation factor Tu (EF-Tu), SelB is expected to control the delivery and release of Sec-tRNA(Sec) to the ribosome by the structural switch between GTP- and GDP-bound conformations. Guanosine Diphosphate 172-175 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 36-41 22378069-3 2012 Interestingly, S21 belongs to the first eEF1A GTP/GDP-binding consensus sequence. Guanosine Diphosphate 50-53 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 40-45 21665947-1 2011 Translation elongation in eukaryotes is mediated by the concerted actions of elongation factor 1A (eEF1A), which delivers aminoacylated tRNA to the ribosome; elongation factor 1B (eEF1B) complex, which catalyzes the exchange of GDP to GTP on eEF1A; and eEF2, which facilitates ribosomal translocation. Guanosine Diphosphate 228-231 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 99-104 20838377-5 2011 Notably, eEF1A has GTPase activity and can exist in GTP- or GDP-bound forms, which are associated with distinct structural conformations of the protein. Guanosine Diphosphate 60-63 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 9-14 20838377-6 2011 Here, we show that the guanine nucleotide-bound state of eEF1A regulates its ability to activate SK1, with eEF1A.GDP, but not eEF1A.GTP, enhancing SK1 activity in vitro. Guanosine Diphosphate 113-116 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 57-62 20838377-6 2011 Here, we show that the guanine nucleotide-bound state of eEF1A regulates its ability to activate SK1, with eEF1A.GDP, but not eEF1A.GTP, enhancing SK1 activity in vitro. Guanosine Diphosphate 113-116 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 107-112 20838377-6 2011 Here, we show that the guanine nucleotide-bound state of eEF1A regulates its ability to activate SK1, with eEF1A.GDP, but not eEF1A.GTP, enhancing SK1 activity in vitro. Guanosine Diphosphate 113-116 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 107-112 20838377-7 2011 Furthermore, we show that enhancing cellular eEF1A.GDP levels through expression of a guanine nucleotide dissociation inhibitor of eEF1A, translationally controlled tumour protein (TCTP), increased SK1 activity in cells. Guanosine Diphosphate 51-54 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 45-50 20838377-7 2011 Furthermore, we show that enhancing cellular eEF1A.GDP levels through expression of a guanine nucleotide dissociation inhibitor of eEF1A, translationally controlled tumour protein (TCTP), increased SK1 activity in cells. Guanosine Diphosphate 51-54 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens 131-136