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  Structural basis for interaction of the ribosome with the switch regions of GTP-bound elongation factors

Connell, S. R., Takemoto, C., Wilson, D. N., Wang, H., Murayama, K., Terada, T., et al. (2007). Structural basis for interaction of the ribosome with the switch regions of GTP-bound elongation factors. Molecular Cell, 25(5), 751-764. doi:10.1016/j.molcel.2007.01.027.

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Genre: Journal Article
Alternative Title : Mol Cell

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 Creators:
Connell, Sean R.1, Author              
Takemoto, Chie, Author
Wilson, Daniel N.1, Author              
Wang, Hongfei, Author
Murayama, Kazutaka, Author
Terada, Takaho, Author
Shirouzu, Mikako, Author
Rost, Maximilian, Author
Schüler, Martin, Author
Giesebrecht, Jan, Author
Dabrowski, Marylena, Author
Mielke, Thorsten2, Author              
Fucini, Paola3, Author              
Yokoyama, Shigeyuki, 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              
2Imaging/Electron Microscopy (Head: Rudi Lurz/Thorsten Mielke), Scientific Service (Head: Manuela B. Urban), Max Planck Institute for Molecular Genetics, Max Planck Society, ou_1479668              
3Ribosomes, Max Planck Institute for Molecular Genetics, Max Planck Society, ou_1433558              

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Free keywords: RNA
 Abstract: 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.

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Language(s): eng - English
 Dates: 2007-03-09
 Publication Status: Published in print
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Type: -
 Identifiers: eDoc: 334066
DOI: 10.1016/j.molcel.2007.01.027
 Degree: -

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Title: Molecular Cell
  Alternative Title : Mol Cell
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: -
Pages: - Volume / Issue: 25 (5) Sequence Number: - Start / End Page: 751 - 764 Identifier: ISSN: 1097-2765