Mechanisms of EF-Tu, a pioneer GTPase.
This review considers several aspects of the function of EF-Tu, a protein that has greatly contributed to the advancement of our knowledge of both protein biosynthesis and GTP-binding proteins in general. A number of topics are described with emphasis on the function-structure relationships, in particular of EF-Tu's domains, the nucleotide-binding site, and the magnesium-binding network. Aspects related to the interaction with macromolecular ligands and antibiotics and to folding and GTPase activity are also presented and discussed. Comments and criticism are offered to draw attention to remaining discrepancies and problems.
Krab
Ivo M
IM
Laboratory of Biophysics, Ecole Polytechnique, Palaiseau, France.
Parmeggiani
Andrea
A
D000595:Amino Acid Sequence; D000900:Anti-Bacterial Agents / Q000494:pharmacology; D001665:Binding Sites; D008958:Models, Molecular; D008969:Molecular Sequence Data; D010441:Peptide Chain Elongation, Translational; D010444:Peptide Elongation Factor Tu / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D011487:Protein Conformation; D017434:Protein Structure, Tertiary; D011500:Protein Synthesis Inhibitors / Q000494:pharmacology
D000900:Anti-Bacterial Agents; D011500:Protein Synthesis Inhibitors; D010444:Peptide Elongation Factor Tu