Research Article

The Structure of the Ribosome with Elongation Factor G Trapped in the Posttranslocational State

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Science  30 Oct 2009:
Vol. 326, Issue 5953, pp. 694-699
DOI: 10.1126/science.1179709

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Elongation factor G (EF-G) is a guanosine triphosphatase (GTPase) that plays a crucial role in the translocation of transfer RNAs (tRNAs) and messenger RNA (mRNA) during translation by the ribosome. We report a crystal structure refined to 3.6 angstrom resolution of the ribosome trapped with EF-G in the posttranslocational state using the antibiotic fusidic acid. Fusidic acid traps EF-G in a conformation intermediate between the guanosine triphosphate and guanosine diphosphate forms. The interaction of EF-G with ribosomal elements implicated in stimulating catalysis, such as the L10-L12 stalk and the L11 region, and of domain IV of EF-G with the tRNA at the peptidyl-tRNA binding site (P site) and with mRNA shed light on the role of these elements in EF-G function. The stabilization of the mobile stalks of the ribosome also results in a more complete description of its structure.

  • * Present address: Department of Cell and Molecular Biology, Uppsala University, Box 596, Uppsala, SE 751 24, Sweden.

  • Present address: Department of Biochemistry, Emory University School of Medicine, Atlanta, GA 30322, USA.

  • Present address: The Rockefeller University, Box 224, New York, NY 10065, USA.

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