Molecular Cell, volume 25, issue 5, pages 751-764

Structural Basis for Interaction of the Ribosome with the Switch Regions of GTP-Bound Elongation Factors

Connell Sean D. 1
Takemoto Chie 2
Wang Howard 2
MURAYAMA Kouhei 4
Terada Takaho 2
SHIROUZU Mikako 2
Rost Maximilian 1
Schuler Martin 1
Giesebrecht Jan 1
Dabrowski Marylena 1
Mielke Thorsten 5
Fucini Paola 6
YOKOYAMA Shigeyuki 7
Spahn Christian M. T. 3
1
 
Institut für Medizinische Physik und Biophysik, Charite – Universitätsmedizin Berlin, Ziegelstrasse 5-9, 10117-Berlin, Germany
2
 
RIKEN Genomic Sciences Center, 1-7-22 Suehiro-cho, Tsurumi, Yokohama 230-0045, Japan
4
 
Tohoku University Biomedical Engineering Research Organization, 2-1 Seiryo-machi, Aoba-ku, Sendai 980-8575, Japan
6
 
Ribosomes, Max Planck Institute for Molecular Genetics, Max Planck Society
Publication typeJournal Article
Publication date2007-03-09
Journal: Molecular Cell
Quartile SCImago
Q1
Quartile WOS
Q1
Impact factor16
ISSN10972765, 10974164
Molecular Biology
Cell Biology
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 A resolution and the crystal structure of EF-G-2*GTP, an EF-G homolog, at 2.2 A 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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Connell S. D. et al. Structural Basis for Interaction of the Ribosome with the Switch Regions of GTP-Bound Elongation Factors // Molecular Cell. 2007. Vol. 25. No. 5. pp. 751-764.
GOST all authors (up to 50) Copy
Connell S. D., Takemoto C., Wilson D. W., Wang H., MURAYAMA K., Terada T., SHIROUZU M., Rost M., Schuler M., Giesebrecht J., Dabrowski M., Mielke T., Fucini P., YOKOYAMA S., Spahn C. M. T. Structural Basis for Interaction of the Ribosome with the Switch Regions of GTP-Bound Elongation Factors // Molecular Cell. 2007. Vol. 25. No. 5. pp. 751-764.
RIS |
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RIS Copy
TY - JOUR
DO - 10.1016/j.molcel.2007.01.027
UR - https://doi.org/10.1016%2Fj.molcel.2007.01.027
TI - Structural Basis for Interaction of the Ribosome with the Switch Regions of GTP-Bound Elongation Factors
T2 - Molecular Cell
AU - Connell, Sean D.
AU - Takemoto, Chie
AU - Wilson, Daniel W.
AU - Wang, Howard
AU - MURAYAMA, Kouhei
AU - Terada, Takaho
AU - SHIROUZU, Mikako
AU - Rost, Maximilian
AU - Schuler, Martin
AU - Giesebrecht, Jan
AU - Dabrowski, Marylena
AU - Mielke, Thorsten
AU - Fucini, Paola
AU - YOKOYAMA, Shigeyuki
AU - Spahn, Christian M. T.
PY - 2007
DA - 2007/03/09 00:00:00
PB - Elsevier
SP - 751-764
IS - 5
VL - 25
SN - 1097-2765
SN - 1097-4164
ER -
BibTex |
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BibTex Copy
@article{2007_Connell
author = {Sean D. Connell and Chie Takemoto and Daniel W. Wilson and Howard Wang and Kouhei MURAYAMA and Takaho Terada and Mikako SHIROUZU and Maximilian Rost and Martin Schuler and Jan Giesebrecht and Marylena Dabrowski and Thorsten Mielke and Paola Fucini and Shigeyuki YOKOYAMA and Christian M. T. Spahn},
title = {Structural Basis for Interaction of the Ribosome with the Switch Regions of GTP-Bound Elongation Factors},
journal = {Molecular Cell},
year = {2007},
volume = {25},
publisher = {Elsevier},
month = {mar},
url = {https://doi.org/10.1016%2Fj.molcel.2007.01.027},
number = {5},
pages = {751--764},
doi = {10.1016/j.molcel.2007.01.027}
}
MLA
Cite this
MLA Copy
Connell, Sean D., et al. “Structural Basis for Interaction of the Ribosome with the Switch Regions of GTP-Bound Elongation Factors.” Molecular Cell, vol. 25, no. 5, Mar. 2007, pp. 751-764. https://doi.org/10.1016%2Fj.molcel.2007.01.027.
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