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



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ID: 305607.0, MPI für molekulare Genetik / Department of Vertebrate Genomics
Structure of eEF3 and the mechanism of transfer RNA release from the E-site
Authors:Andersen, Christian B. F.; Becker, Thomas.; Blau, Michael; Anand, Monika; Halic, Mario; Balar, Bharvi; Mielke, Thorsten; Boesen, Thomas; Pedersen, Jan Skov; Spahn, Christian M. T.; Kinzy, Terri Goss; Andersen, Gregers R.; Beckmann, Roland
Language:English
Date of Publication (YYYY-MM-DD):2006-10-12
Title of Journal:Nature
Volume:443
Issue / Number:7112
Start Page:663
End Page:668
Copyright:© 2007 Nature Publishing Group
Review Status:not specified
Audience:Experts Only
Abstract / Description:Elongation factor eEF3 is an ATPase that, in addition to the two canonical factors eEF1A and eEF2, serves an essential function in the translation cycle of fungi. eEF3 is required for the binding of the aminoacyl-tRNA–eEF1A–GTP ternary complex to the ribosomal A-site and has been suggested to facilitate the clearance of deacyl-tRNA from the E-site. Here we present the crystal structure of Saccharomyces cerevisiae eEF3, showing that it consists of an amino-terminal HEAT repeat domain, followed by a four-helix bundle and two ABC-type ATPase domains, with a chromodomain inserted in ABC2. Moreover, we present the cryo-electron microscopy structure of the ATP-bound form of eEF3 in complex with the post-translocational-state 80S ribosome from yeast. eEF3 uses an entirely new factor binding site near the ribosomal E-site, with the chromodomain likely to stabilize the ribosomal L1 stalk in an open conformation, thus allowing tRNA release.
Comment of the Author/Creator:Correspondence to: Gregers R. Andersen, Roland Beckmann; Correspondence and requests for materials should be addressed to R.B.(Email: beckmann@lmb.uni-muenchen.de) and G.R.A. (Email: gra@mb.au.dk)
External Publication Status:published
Document Type:Article
Communicated by:Hans Lehrach
Affiliations:MPI für molekulare Genetik
External Affiliations:1. Centre for Structural Biology, Department of Molecular Biology, University of Aarhus, Gustav Wieds Vej 10C, DK-8000 Aarhus, Denmark;
2. Institute of Biochemistry, Charité, University Medical School, Humboldt University of Berlin, Monbijoustrasse 2, 10117 Berlin, Germany;
3. Department of Molecular Genetics, Microbiology & Immunology, UMDNJ Robert Wood Johnson Medical School, Piscataway, New Jersey 08854-5635, USA;
4. UltraStructureNetwork, USN, Max Planck Institute for Molecular Genetics, Ihnestrasse 63-73, 14195 Berlin, Germany;
5. Department of Chemistry and iNANO Interdisciplinary Nanoscience Center, University of Aarhus, Langelandsgade 140, DK-8000 Aarhus, Denmark;
6. Institut für Medizinische Physik und Biophysik, Charité, University Medical School, Humboldt University of Berlin, Ziegelstrasse 5-9, 10117 Berlin, Germany;
7. Present address: Gene Center and Department of Chemistry & Biochemistry, University of Munich, Feodor-Lynen-Strasse 25, 81377 Munich, Germany;
8. These authors contributed equally to this work
Identifiers:ISSN:0028-0836
DOI:10.1038/nature05126
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