Title : The conformational properties of elongation factor G and the mechanism of translocation.

Pub. Date : 1997 Aug 19

PMID : 9254632






7 Functional Relationships(s)
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1 Crystallographic investigations have revealed that EF-G.GDP resembles the EF-Tu.GTP. Guanosine Diphosphate G elongation factor mitochondrial 1 Homo sapiens
2 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 G elongation factor mitochondrial 1 Homo sapiens
3 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 G elongation factor mitochondrial 1 Homo sapiens
4 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 G elongation factor mitochondrial 1 Homo sapiens
5 The data show that nucleotide-free EF-G, EF-G.GDP, EF-G. Guanosine Diphosphate G elongation factor mitochondrial 1 Homo sapiens
6 The data show that nucleotide-free EF-G, EF-G.GDP, EF-G. Guanosine Diphosphate G elongation factor mitochondrial 1 Homo sapiens
7 GTP, and EF-G.GMPPCP cannot be distinguished by solution scattering and that it is likely they all resemble crystalline EF-G.GDP. Guanosine Diphosphate G elongation factor mitochondrial 1 Homo sapiens