A complex profile of protein elongation: translating chemical energy into molecular movement.
The recently solved structures of the protein elongation factor complexes, EF-Tu-GDPNP-phenylalanyl-tRNA and EF-T-Ts, complete the atomic profile of four EF-Tu conformational states. As a set, the three-dimensional structures suggest an atomic model for movement during protein elongation and, by molecular mimicry with EF-G, translocation as well.
Abel
K
K
Department of Biochemistry, University of California, Riverside, CA 92507, USA.
Jurnak
F
F
D006153:Guanosine Diphosphate / Q000378:metabolism / Q000502:physiology; D008958:Models, Molecular; D018716:Molecular Mimicry; D015394:Molecular Structure; D010441:Peptide Chain Elongation, Translational / Q000502:physiology*; D010444:Peptide Elongation Factor Tu / Q000737:chemistry*; D010445:Peptide Elongation Factors / Q000737:chemistry*; D011487:Protein Conformation; D012360:RNA, Transfer, Phe / Q000378:metabolism; D012270:Ribosomes / Q000502:physiology
D010445:Peptide Elongation Factors; D012360:RNA, Transfer, Phe; C023512:elongation factor Ts; D006153:Guanosine Diphosphate; D010444:Peptide Elongation Factor Tu