The mechanism for activation of GTP hydrolysis on the ribosome

Science

Volumn 330, Issue 6005, 2010, Pages 835-838

  Voorhees, Rebecca M ^a   Schmeing, T Martin ^a,b   Kelley, Ann C ^a   Ramakrishnan, V ^a  

^a MRC LABORATORY OF MOLECULAR BIOLOGY   (United Kingdom)

^b MCGILL UNIVERSITY   (Canada)

Author keywords

[No Author keywords available]

Indexed keywords

AMINOACYL TRANSFER RNA; ELONGATION FACTOR TU; GUANOSINE TRIPHOSPHATASE; GUANOSINE TRIPHOSPHATE; HISTIDINE; RNA 23S; TRANSFER RNA; WATER;

CRYSTAL STRUCTURE; ENZYME ACTIVITY; EXPERIMENTAL STUDY; HYDROLYSIS; PROTEIN;

ARTICLE; CATALYSIS; CONFORMATIONAL TRANSITION; CRYSTAL STRUCTURE; ENZYME ACTIVATION; HYDROLYSIS; PRIORITY JOURNAL; PROTEIN INTERACTION; RIBOSOME;

BACTERIAL PROTEINS; CATALYTIC DOMAIN; CRYSTALLOGRAPHY, X-RAY; ENZYME ACTIVATION; GUANOSINE TRIPHOSPHATE; HYDROLYSIS; HYDROPHOBIC AND HYDROPHILIC INTERACTIONS; NUCLEIC ACID CONFORMATION; PAROMOMYCIN; PEPTIDE ELONGATION FACTOR TU; PHOSPHATES; PROTEIN STRUCTURE, TERTIARY; RIBOSOMES; RNA, BACTERIAL; RNA, RIBOSOMAL, 23S; RNA, TRANSFER, AMINO ACYL; THERMUS THERMOPHILUS;

EID: 78149302861     PISSN: 00368075     EISSN: 10959203     Source Type: Journal    
DOI: 10.1126/science.1194460     Document Type: Article

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35. We thank R. Green for reagents and D. de Sanctis at the European Synchrotron Radiation Facility for facilitating data collection. This work was supported by the Medical Research Council UK, the Wellcome Trust, the Agouron Institute, and the Louis-Jeantet Foundation. R.M.V. is supported by a Gates-Cambridge scholarship, and T.M.S. by the Human Frontier Science Program and Emmanuel College. V.R. is on the Scientific Advisory Board and holds stock options in Rib-X pharmaceuticals. Transfer of Thermus thermophilis ribosome strain T.th. HB8-MRC-MSAW1 requires a Materials Transfer Agreement with the MRC. Coordinates and structure factors have been deposited at the Protein Data Bank with accession codes 2xqd and 2xqe.