The Structure of the Ribosome with Elongation Factor G Trapped in the Posttranslocational State
- 30 October 2009
- journal article
- research article
- Published by American Association for the Advancement of Science (AAAS) in Science
- Vol. 326 (5953), 694-699
- https://doi.org/10.1126/science.1179709
Abstract
Ribosomes Caught in Translation: To synthesize proteins, the ribosome must select cognate transfer RNAs (tRNAs) based on base-pairing with the messenger RNA (mRNA) template (a process known as decoding), form a peptide bond, and then move the mRNA:tRNA assembly relative to the ribosome (a process known as translocation). Decoding and translocation require protein guanosine triphosphatases (GTPases), and, while high-resolution structures of the ribosome have greatly furthered our understanding of ribosome function, the detailed mechanism of these GTPases during the elongation cycle remains unclear. Two Research Articles now give a clearer view of these steps in bacterial protein synthesis (see the Perspective by Liljas ). Schmeing et al. (p. 688 , published online 15 October) present the crystal structure of the ribosome bound to Elongation factor-Tu (EF-Tu) and amino-acyl tRNA that gives insight into how EF-Tu contributes to accurate decoding. Gao et al. (p. 694 , published online 15 October) describe the crystal structure of the ribosome bound to Elongation factor-G (EF-G) trapped in a posttranslocation state by the antibiotic fusidic acid that gives insight into how EF-G functions in translocation.Keywords
This publication has 44 references indexed in Scilit:
- Insights into substrate stabilization from snapshots of the peptidyl transferase center of the intact 70S ribosomeNature Structural & Molecular Biology, 2009
- Visualization of the Hybrid State of tRNA Binding Promoted by Spontaneous Ratcheting of the RibosomeMolecular Cell, 2008
- Crystallographic Analysis of Human Serum Albumin Complexed with 4Z,15E-Bilirubin-IXαJournal of Molecular Biology, 2008
- Translational Regulation via L11: Molecular Switches on the Ribosome Turned On and Off by Thiostrepton and MicrococcinMolecular Cell, 2008
- Kinetically Competent Intermediates in the Translocation Step of Protein SynthesisMolecular Cell, 2007
- Structure of the 70 S Ribosome Complexed with mRNA and tRNAScience, 2006
- Interaction of the G′ Domain of Elongation Factor G and the C-Terminal Domain of Ribosomal Protein L7/L12 during Translocation as Revealed by Cryo-EMMolecular Cell, 2005
- Structural Insights into Fusidic Acid Resistance and Sensitivity in EF-GJournal of Molecular Biology, 2005
- Conformational Changes of the Small Ribosomal Subunit During Elongation Factor G-dependent tRNA–mRNA TranslocationJournal of Molecular Biology, 2004
- Hydrolysis of GTP by elongation factor G drives tRNA movement on the ribosomeNature, 1997