Title : Elongation Factor Tu's Nucleotide Binding Is Governed by a Thermodynamic Landscape Unique among Bacterial Translation Factors.

Pub. Date : 2019 Jul 3

PMID : 31058500






4 Functional Relationships(s)
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1 EF-Tu alternates between GTP- and GDP-bound conformations during its functional cycle, representing the "on" and "off" states, respectively. Guanosine Diphosphate eukaryotic translation elongation factor 1 alpha 1 Homo sapiens
2 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 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens
3 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 eukaryotic translation elongation factor 1 alpha 1 Homo sapiens
4 GDP binding to the apo conformation of EF-Tu is both enthalpically and entropically favored, a feature unique among translational GTPases. Guanosine Diphosphate eukaryotic translation elongation factor 1 alpha 1 Homo sapiens