PMID:9600930
| Citation |
Agrawal, RK, Penczek, P, Grassucci, RA and Frank, J (1998) Visualization of elongation factor G on the Escherichia coli 70S ribosome: the mechanism of translocation. Proc. Natl. Acad. Sci. U.S.A. 95:6134-8 |
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| Abstract |
During protein synthesis, elongation factor G (EF-G) binds to the ribosome and promotes the step of translocation, a process in which tRNA moves from the A to the P site of the ribosome and the mRNA is advanced by one codon. By using three-dimensional cryo-electron microscopy, we have visualized EF-G in a ribosome-EF-G-GDP-fusidic acid complex. Fitting the crystal structure of EF-G-GDP into the cryo density map reveals a large conformational change mainly associated with domain IV, the domain that mimics the shape of the anticodon arm of the tRNA in the structurally homologous ternary complex of Phe-tRNAPhe, EF-Tu, and a GTP analog. The tip portion of this domain is found in a position that overlaps the anticodon arm of the A-site tRNA, whose position in the ribosome is known from a study of the pretranslocational complex, implying that EF-G displaces the A-site tRNA to the P site by physical interaction with the anticodon arm. |
| Links | |
| Keywords |
Crystallography, X-Ray; Escherichia coli/genetics; Escherichia coli/metabolism; Escherichia coli/ultrastructure; Peptide Elongation Factor G; Peptide Elongation Factors/chemistry; Peptide Elongation Factors/genetics; Peptide Elongation Factors/ultrastructure; Protein Biosynthesis; Protein Conformation; Ribosomes/chemistry; Ribosomes/genetics; Ribosomes/ultrastructure |
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