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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Cate, Jamie H. D. Pulk, Arto |
| Description | Author Affiliation: Pulk A ( Department of Molecular and Cell Biology, California Institute for Quantitative Biosciences, University of California, Berkeley, CA 94720, USA.) |
| Abstract | Protein synthesis by the ribosome requires the translocation of transfer RNAs and messenger RNA by one codon after each peptide bond is formed, a reaction that requires ribosomal subunit rotation and is catalyzed by the guanosine triphosphatase (GTPase) elongation factor G (EF-G). We determined 3 angstrom resolution x-ray crystal structures of EF-G complexed with a nonhydrolyzable guanosine 5'-triphosphate (GTP) analog and bound to the Escherichia coli ribosome in different states of ribosomal subunit rotation. The structures reveal that EF-G binding to the ribosome stabilizes switch regions in the GTPase active site, resulting in a compact EF-G conformation that favors an intermediate state of ribosomal subunit rotation. These structures suggest that EF-G controls the translocation reaction by cycles of conformational rigidity and relaxation before and after GTP hydrolysis. |
| ISSN | 00368075 |
| e-ISSN | 10959203 |
| Journal | Science |
| Issue Number | 6140 |
| Volume Number | 340 |
| Language | English |
| Publisher | American Association for the Advancement of Science (United States) |
| Publisher Date | 2013-06-28 |
| Publisher Place | United States |
| Access Restriction | Open |
| Subject Keyword | Escherichia Coli Enzymology Guanosine Triphosphate Chemistry Peptide Elongation Factor G Protein Biosynthesis Ribosome Subunits, Large, Bacterial Crystallography, X-Ray Hydrolysis Models, Biological Protein Conformation Protein Structure, Tertiary RNA, Messenger RNA, Transfer Rotation Research Support, N.I.H., Extramural Research Support, U.S. Gov't, Non-P.H.S. Multidisciplinary |
| Content Type | Text |
| Resource Type | Article |
| Subject | History and Philosophy of Science |
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