The crystal structure of the ribosome bound to EF-Tu and aminoacyl-tRNA

Science

Volumn 326, Issue 5953, 2009, Pages 688-694

  Martin Schmeing, T ^a   Voorhees, Rebecca M ^a   Kelley, Ann C ^a   Gao, Yong Gui ^a   Murphy IV, Frank V ^b   Weir, John R ^c   Ramakrishnan, V ^a  

^a MRC LABORATORY OF MOLECULAR BIOLOGY   (United Kingdom)

^b ARGONNE NATIONAL LABORATORY   (United States)

^c MAX PLANCK INSTITUTE OF BIOCHEMISTRY   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

AMINOACYL TRANSFER RNA; ELONGATION FACTOR TU; GUANOSINE TRIPHOSPHATASE; NUCLEOTIDE; RNA 16S; TRANSFER RNA;

AMINO ACID; CRYSTAL STRUCTURE; ENZYME ACTIVITY; HYDROLYSIS; PEPTIDE; RNA;

ARTICLE; BINDING SITE; CODON; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; CRYSTAL STRUCTURE; DISTORTION PRODUCT OTOACOUSTIC EMISSION; ENZYME ACTIVATION; HUMAN; NONHUMAN; PRIORITY JOURNAL; PROTEIN INTERACTION; RIBOSOME; STRUCTURE ANALYSIS;

CRYSTALLOGRAPHY, X-RAY; ENZYME ACTIVATION; GENETIC CODE; GTP PHOSPHOHYDROLASES; MODELS, MOLECULAR; NUCLEIC ACID CONFORMATION; PEPTIDE ELONGATION FACTOR TU; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN STRUCTURE, TERTIARY; RIBOSOMES; RNA, BACTERIAL; RNA, TRANSFER, AMINO ACYL; RNA, TRANSFER, PHE; RNA, TRANSFER, THR; THERMUS THERMOPHILUS;

EID: 70350588648     PISSN: 00368075     EISSN: 10959203     Source Type: Journal    
DOI: 10.1126/science.1179700     Document Type: Article

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46. 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 dillraction 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 Kb-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.