The Crystal Structure of the Ribosome Bound to EF-Tu and Aminoacyl-tRNA
Abstract
The ribosome selects a correct transfer RNA (tRNA) for each amino acid added to the polypeptide chain, as directed by messenger RNA. Aminoacyl-tRNA is delivered to the ribosome by elongation factor Tu (EF-Tu), which hydrolyzes guanosine triphosphate (GTP) and releases tRNA in response to codon recognition. The signaling pathway that leads to GTP hydrolysis upon codon recognition is critical to accurate decoding. Here we present the crystal structure of the ribosome complexed with EF-Tu and aminoacyl-tRNA, refined to 3.6 angstrom resolution. The structure reveals details of the tRNA distortion that allows aminoacyl-tRNA to interact simultaneously with the decoding center of the 30S subunit and EF-Tu at the factor binding site. A series of conformational changes in EF-Tu and aminoacyl-tRNA suggests a communication pathway between the decoding center and the guanosine triphosphatase center of EF-Tu.
Additional Information
© 2009 American Association for the Advancement of Science. Received 27 July 2009; accepted 9 September 2009. Published online 15 October 2009. We thank M. M. Babu and P. Lukavski for help with data analysis, G. Leonard and S. Brockhauser for their guidance and advice with data collection at the European Synchrotron Light Source beamline ID14.4, C. Schulze-Briese and A. Pauluhn for help with initial diffraction studies performed at the Swiss Light Source, and L. Ulisko for preparation of additional images. This work was supported by the Medical Research Council U.K., the Wellcome Trust, the Agouron Institute, and the Louis-Jeantet Foundation. R.M.V. is the recipient of a Gates-Cambridge scholarship; T.M.S. received support from the Human Frontiers Science Program Organization and Emmanuel College, University of Cambridge; and V.R. holds stock options and is on the Scientific Advisory Board of Rib-X Pharmaceuticals, a company dedicated to making antibiotics that target the ribosome. The structure has been deposited at the Protein Data Bank with accession codes 2WRN, 2WRO, 2WRQ, and 2WRR.Attached Files
Accepted Version - emss-54561.pdf
Supplemental Material - 1179700s1.mov
Supplemental Material - Schmeing.SOM.pdf
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Additional details
- PMCID
- PMC3763470
- Eprint ID
- 84342
- DOI
- 10.1126/science.1179700
- Resolver ID
- CaltechAUTHORS:20180116-104121492
- Medical Research Council (UK)
- Wellcome Trust
- Agouron Institute
- Louis-Jeantet Foundation
- Gates-Cambridge Scholarship
- Human Frontier Science Program
- University of Cambridge
- Created
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2018-01-17Created from EPrint's datestamp field
- Updated
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2023-02-28Created from EPrint's last_modified field