Note to users. If you're seeing this message, it means that your browser cannot find this page's style/presentation instructions -- or possibly that you are using a browser that does not support current Web standards. Find out more about why this message is appearing, and what you can do to make your experience of our site the best it can be.

Originally published in Science Express on 15 October 2009
Science 30 October 2009:
Vol. 326. no. 5953, pp. 694 - 699
DOI: 10.1126/science.1179709
Prev | Table of Contents | Next

Research Articles

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

Yong-Gui Gao, Maria Selmer,* Christine M. Dunham,{dagger} Albert Weixlbaumer,{ddagger} Ann C. Kelley, V. Ramakrishnan§

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.

MRC Laboratory of Molecular Biology, Hills Road, Cambridge, CB2 0QH, UK.

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

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

{ddagger} Present address: The Rockefeller University, Box 224, New York, NY 10065, USA.

§ To whom correspondence should be addressed. E-mail: ramak{at}mrc-lmb.cam.ac.uk

Read the Full Text


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
Leaps in Translational Elongation.
A. Liljas (2009)
Science 326, 677-678
   Abstract »    Full Text »    PDF »


To Advertise     Find Products

Science. ISSN 0036-8075 (print), 1095-9203 (online)