The structure of the ribosome with elongation factor g trapped in the posttranslocational state

Science

Volumn 326, Issue 5953, 2009, Pages 694-699

  Gao, Yong Gui ^a   Selmer, Maria ^b   Dunham, Christine M ^c   Weixlbaumer, Albert ^d   Kelley, Ann C ^a   Ramakrishnan, V ^a  

^a MRC LABORATORY OF MOLECULAR BIOLOGY   (United Kingdom)

^b UPPSALA UNIVERSITY   (Sweden)

^c EMORY UNIVERSITY SCHOOL OF MEDICINE   (United States)

^d ROCKEFELLER UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ELONGATION FACTOR G; FUSIDIC ACID; GUANOSINE DIPHOSPHATE; GUANOSINE TRIPHOSPHATE; MESSENGER RNA; TRANSFER RNA;

ANTIBIOTICS; CATALYSIS; CRYSTAL STRUCTURE; ENZYME ACTIVITY; PHOSPHATE; RNA; TRANSLOCATION;

ARTICLE; CATALYSIS; CHEMICAL STRUCTURE; CRYSTAL STRUCTURE; CRYSTALLIZATION; NONHUMAN; PRIORITY JOURNAL; RIBOSOME;

BACTERIAL PROTEINS; CATALYSIS; CRYSTALLOGRAPHY, X-RAY; FUSIDIC ACID; MODELS, MOLECULAR; PEPTIDE ELONGATION FACTOR G; PROTEIN BIOSYNTHESIS; PROTEIN CONFORMATION; PROTEIN STRUCTURE, TERTIARY; PROTEIN SYNTHESIS INHIBITORS; RIBOSOMES; RNA, BACTERIAL; RNA, MESSENGER; RNA, TRANSFER; THERMUS THERMOPHILUS;

EID: 70350602056     PISSN: 00368075     EISSN: 10959203     Source Type: Journal    
DOI: 10.1126/science.1179709     Document Type: Article

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50. We thank C. Schulze-Briese, M. Fuchs, and M. Wang for help with data collection at the Swiss Light Source; J. Frank for coordinates of the ratcheted ribosome obtained from modeling into cryo-EM maps; J. Hentschel for help with crystallization trials; M. Schmeing and R. Voorhees for help with data collection, making figures, and critical feedback; and C. Neubauer and L. Ng for useful discussions. V.R. was supported by the U.K. Medical Research Council, a Wellcome Trust program grant, and awards from the Agouron Institute and the Louis-Jeantet Foundation. Coordinates for the structure have been deposited in the Protein Data Bank as four split entries with codes 2wri, 2wrj, 2wrk, and 2wrl.