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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: Zeitschriftenartikel
Alternativer Titel : Mol Cell

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 Urheber:
Connell, Sean R.1, Autor           
Takemoto, Chie, Autor
Wilson, Daniel N.1, Autor           
Wang, Hongfei, Autor
Murayama, Kazutaka, Autor
Terada, Takaho, Autor
Shirouzu, Mikako, Autor
Rost, Maximilian, Autor
Schüler, Martin, Autor
Giesebrecht, Jan, Autor
Dabrowski, Marylena, Autor
Mielke, Thorsten2, Autor           
Fucini, Paola3, Autor           
Yokoyama, Shigeyuki, Autor
Spahn, Christian M. T.1, Autor           
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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Schlagwörter: RNA
 Zusammenfassung: 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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Sprache(n): eng - English
 Datum: 2007-03-09
 Publikationsstatus: Erschienen
 Seiten: -
 Ort, Verlag, Ausgabe: -
 Inhaltsverzeichnis: -
 Art der Begutachtung: -
 Identifikatoren: eDoc: 334066
DOI: 10.1016/j.molcel.2007.01.027
 Art des Abschluß: -

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Titel: Molecular Cell
  Alternativer Titel : Mol Cell
Genre der Quelle: Zeitschrift
 Urheber:
Affiliations:
Ort, Verlag, Ausgabe: -
Seiten: - Band / Heft: 25 (5) Artikelnummer: - Start- / Endseite: 751 - 764 Identifikator: ISSN: 1097-2765