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

ID: 457398.0, MPI für molekulare Genetik / Department of Vertebrate Genomics
GTPase activation of elongation factor EF-Tu by the ribosome during decoding.
Authors:Jan-Christian Schuette, Jan-Christian; Murphy, Frank V.; Kelley, Ann C.; Weir, John R.; Giesebrecht, Jan; Connell, Sean R.; Loerke, Justus; Mielke, Thorsten; Zhang, Wei; Penczek, Pawel A.; Ramakrishnan, V.; Spahn, Christian M. T.
Date of Publication (YYYY-MM-DD):2009-02-19
Title of Journal:The EMBO Journal
Journal Abbrev.:EMBO
Issue / Number:6
Start Page:755
End Page:765
Copyright:The Author 2009. Published by Oxford University Press. All rights reserved. For Permissions, please email: journals.permissions@oxfordjournals.
Review Status:not specified
Audience:Experts Only
Abstract / Description:We have used single-particle reconstruction in cryo-electron microscopy to determine a structure of the Thermus thermophilus ribosome in which the ternary complex of elongation factor Tu (EF-Tu), tRNA and guanine nucleotide has been trapped on the ribosome using the antibiotic kirromycin. This represents the state in the decoding process just after codon recognition by tRNA and the resulting GTP hydrolysis by EF-Tu, but before the release of EF-Tu from the ribosome. Progress in sample purification and image processing made it possible to reach a resolution of 6.4 Å. Secondary structure elements in tRNA, EF-Tu and the ribosome, and even GDP and kirromycin, could all be visualized directly. The structure reveals a complex conformational rearrangement of the tRNA in the A/T state and the interactions with the functionally important switch regions of EF-Tu crucial to GTP hydrolysis. Thus, the structure provides insights into the molecular mechanism of signalling codon recognition from the decoding centre of the 30S subunit to the GTPase centre of EF-Tu.
Free Keywords:cryo-electron microscopy;
elongation factor;
Comment of the Author/Creator:Correspondence to:
V Ramakrishnan, MRC Laboratory of Molecular Biology, Hills Road, Cambridge CB2 0QH, UK. Tel.: +44 1223 402213; Fax: +44 1223 213556; E-mail:

Christian M T Spahn, Institute of Medical Physics and Biophysics, Charite-Universitätsmedizin Berlin, Ziegelstrasse 5-9, 10117 Berlin, Germany. Tel.: +49 30 450 5241 31; Fax: +49 30 450 5249 31; E-mail:
External Publication Status:published
Document Type:Article
Communicated by:Hans Lehrach
Affiliations:MPI für molekulare Genetik
External Affiliations:1.Institut für Medizinische Physik und Biophysik, Charite-Universitätsmedizin Berlin, Berlin, Germany;
2.Structural Studies Division, MRC Laboratory of Molecular Biology, Cambridge, UK;
3.Department of Biochemistry and Molecular Biology, The University of Texas—Houston Medical School, Houston, TX, USA.
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