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  GTPase activation of elongation factor EF-Tu by the ribosome during decoding.

Jan-Christian Schuette, J.-C., Murphy, F. V., Kelley, A. C., Weir, J. R., Giesebrecht, J., Connell, S. R., et al. (2009). GTPase activation of elongation factor EF-Tu by the ribosome during decoding. The EMBO Journal, 28(6), 755-765. doi:10.1038/emboj.2009.26.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0010-7E0A-6 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0010-7E0B-4
Genre: Journal Article
Alternative Title : EMBO

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 Creators:
Jan-Christian Schuette, Jan-Christian, Author
Murphy, Frank V., Author
Kelley, Ann C., Author
Weir, John R., Author
Giesebrecht, Jan, Author
Connell, Sean R.1, Author              
Loerke, Justus2, Author
Mielke, Thorsten3, Author              
Zhang, Wei, Author
Penczek, Pawel A., Author
Ramakrishnan, V., Author
Spahn, Christian M. T.1, Author              
Affiliations:
1Dept. of Vertebrate Genomics (Head: Hans Lehrach), Max Planck Institute for Molecular Genetics, Max Planck Society, ou_1433550              
2Max Planck Society, ou_persistent13              
3Imaging/Electron Microscopy (Head: Rudi Lurz/Thorsten Mielke), Scientific Service (Head: Manuela B. Urban), Max Planck Institute for Molecular Genetics, Max Planck Society, ou_1479668              

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Free keywords: cryo-electron microscopy; elongation factor; GTPase; ribosome; translation
 Abstract: 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.

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Language(s): eng - English
 Dates: 2009-02-19
 Publication Status: Published in print
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Title: The EMBO Journal
  Alternative Title : EMBO
Source Genre: Journal
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Pages: - Volume / Issue: 28 (6) Sequence Number: - Start / End Page: 755 - 765 Identifier: ISSN: 0261-4189