Regulatory GTPases
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Cited by (39)
Translation-Process and control
2021, Emerging Concepts in Ribosome Structure, Biogenesis, and FunctionThermodynamics of the GTP-GDP-operated conformational switch of selenocysteine-specific translation factor SelB
2012, Journal of Biological ChemistryCitation Excerpt :The heat capacity change associated with the GTP-to-GDP switch is 346 cal × mol−1 × K−1, which is larger than that estimated for EF-G (35) and IF2 (34), 250 and 290 cal × mol−1 × K−1, respectively. Part of this rearrangement was suggested to come from alterations in the switch 1 and switch 2 regions of the factors, by analogy to the well documented structural changes observed in EF-Tu and other GTPases (36). However, given the large number of amino acid residues that change their partner during complex formation, i.e. about 25 amino acids in SelB, other structural changes, e.g. in the contacts between domains, are likely to contribute as well.
Structural Basis for Interaction of the Ribosome with the Switch Regions of GTP-Bound Elongation Factors
2007, Molecular CellCitation Excerpt :The cycle then repeats, with EF-Tu delivering a new aa-tRNA as dictated by the codon now exposed in the ribosomal A site. The mechanism of EF-Tu appears to follow the classical scheme of G proteins (Hilgenfeld, 1995; Yokosawa et al., 1973) in that it is active in the GTP bound form and inactive in the GDP bound form: in the GTP form, EF-Tu has high affinity for aa-tRNAs, which is markedly decreased upon GTP hydrolysis. Local conformational changes in the GTP binding pocket of EF-Tu, which are in turn translated into a gross conformational change in the overall structure, are responsible for the change in affinity for aa-tRNA (Nyborg et al., 1996).
Recognition and selection of tRNA in translation
2005, FEBS LettersEssential role of histidine 84 in elongation factor Tu for the chemical step of GTP hydrolysis on the ribosome
2003, Journal of Molecular BiologyTranscriptional regulation at a distance in bacteria
2001, Current Opinion in Microbiology