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The Crystal Structure of the Ribosome Bound to EF-Tu and Aminoacyl-tRNA

Schmeing, T. Martin and Voorhees, Rebecca M. and Kelley, Ann C. and Gao, Yong-Gui and Murphy, Frank V., IV and Weir, John R. and Ramakrishnan, V. (2009) The Crystal Structure of the Ribosome Bound to EF-Tu and Aminoacyl-tRNA. Science, 326 (5953). pp. 688-694. ISSN 0036-8075. PMCID PMC3763470. http://resolver.caltech.edu/CaltechAUTHORS:20180116-104121492

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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.


Item Type:Article
Related URLs:
URLURL TypeDescription
https://doi.org/10.1126/science.1179700DOIArticle
http://science.sciencemag.org/content/326/5953/688PublisherArticle
https://www.sciencemag.org/cgi/content/full/1179700/DC1PublisherSupplemental Materials
https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3763470PubMed CentralArticle
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.
Funders:
Funding AgencyGrant Number
Medical Research Council (UK)UNSPECIFIED
Wellcome TrustUNSPECIFIED
Agouron InstituteUNSPECIFIED
Louis-Jeantet FoundationUNSPECIFIED
Gates-Cambridge ScholarshipUNSPECIFIED
Human Frontier Science ProgramUNSPECIFIED
University of CambridgeUNSPECIFIED
PubMed Central ID:PMC3763470
Record Number:CaltechAUTHORS:20180116-104121492
Persistent URL:http://resolver.caltech.edu/CaltechAUTHORS:20180116-104121492
Official Citation:The Crystal Structure of the Ribosome Bound to EF-Tu and Aminoacyl-tRNA. BY T. MARTIN SCHMEING, REBECCA M. VOORHEES, ANN C. KELLEY, YONG-GUI GAO, FRANK V. MURPHY IV, JOHN R. WEIR, V. RAMAKRISHNAN. Science 30 Oct 2009: Vol. 326, Issue 5953, pp. 688-694 DOI: 10.1126/science.1179700
Usage Policy:No commercial reproduction, distribution, display or performance rights in this work are provided.
ID Code:84342
Collection:CaltechAUTHORS
Deposited By: Tony Diaz
Deposited On:17 Jan 2018 17:49
Last Modified:17 Jan 2018 19:27

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