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          Institute: MPI für molekulare Genetik     Collection: Department of Vertebrate Genomics     Display Documents



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ID: 334066.0, MPI für molekulare Genetik / Department of Vertebrate Genomics
Structural basis for interaction of the ribosome with the switch regions of GTP-bound elongation factors
Authors:Connell, Sean R.; Takemoto, Chie; Wilson, Daniel N.; Wang, Hongfei; Murayama, Kazutaka; Terada, Takaho; Shirouzu, Mikako; Rost, Maximilian; Schüler, Martin; Giesebrecht, Jan; Dabrowski, Marylena; Mielke, Thorsten; Fucini, Paola; Yokoyama, Shigeyuki; Spahn, Christian M. T.
Language:English
Date of Publication (YYYY-MM-DD):2007-03-09
Title of Journal:Molecular Cell
Journal Abbrev.:Mol Cell
Volume:25
Issue / Number:5
Start Page:751
End Page:764
Copyright:© 2008 Elsevier B.V.
Review Status:not specified
Audience:Experts Only
Abstract / Description:Elongation factor G (EF-G) catalyzes tRNA translocation on the ribosome. Here a cryo-EM reconstruction of the 70S•EF-G ribosomal complex at 7.3 Å resolution and the crystal structure of EF-G-2•GTP, an EF-G homolog, at 2.2 Å resolution are presented. EF-G-2•GTP is structurally distinct from previous EF-G structures, and in the context of the cryo-EM structure, the conformational changes are associated with ribosome binding and activation of the GTP binding pocket. The P loop and switch II approach A2660-A2662 in helix 95 of the 23S rRNA, indicating an important role for these conserved bases. Furthermore, the ordering of the functionally important switch I and II regions, which interact with the bound GTP, is dependent on interactions with the ribosome in the ratcheted conformation. Therefore, a network of interaction with the ribosome establishes the active GTP conformation of EF-G and thus facilitates GTP hydrolysis and tRNA translocation.
Free Keywords:RNA
External Publication Status:published
Document Type:Article
Communicated by:Hans Lehrach
Affiliations:MPI für molekulare Genetik
External Affiliations:Institut für Medizinische Physik und Biophysik, Charite—Universitätsmedizin Berlin, Ziegelstrasse 5-9, 10117 Berlin, Germany;
RIKEN Genomic Sciences Center, 1-7-22 Suehiro-cho, Tsurumi, Yokohama 230-0045, Japan;
Tohoku University Biomedical Engineering Research Organization, 2-1 Seiryo-machi, Aoba-ku, Sendai 980-8575, Japan;
Department of Biophysics and Biochemistry, Graduate School of Science, University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo 113-0033, Japan
Identifiers:ISSN:1097-2765
DOI:10.1016/j.molcel.2007.01.027
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