TY - JOUR
T1 - Structural Basis for Interaction of the Ribosome with the Switch Regions of GTP-Bound Elongation Factors
AU - Connell, Sean R.
AU - Takemoto, Chie
AU - Wilson, Daniel N.
AU - Wang, Hongfei
AU - Murayama, Kazutaka
AU - Terada, Takaho
AU - Shirouzu, Mikako
AU - Rost, Maximilian
AU - Schüler, Martin
AU - Giesebrecht, Jan
AU - Dabrowski, Marylena
AU - Mielke, Thorsten
AU - Fucini, Paola
AU - Yokoyama, Shigeyuki
AU - Spahn, Christian M.T.
N1 - Funding Information:
We would like to thank Drs. K. Wilson and N. Polacek for helpful discussions. The present work was supported by grants from the Volkswagen Stiftung (to C.M.T.S.), by the European Union (to C.M.T.S.), and by the Senatsverwaltung für Wissenschaft, Forschung, und Kultur Berlin (UltraStrukturNetwerk and Anwenderzentrum). S.R.C. was supported by a grant from the Alexander von Humboldt Stiftung. We thank N. Kamiya, H. Naitow, Y. Kawano, T. Hikima, H. Nakajima, T. Matsu, and M. Yamamoto for their assistance in the data collection at BL45XP and BL26B1 in SPring-8; M. Kawazoe, A. Tatsuguchi, and R. Ushikoshi for sample preparation; and S. Sekine and T. Kaminishi for technical assistance. This work was supported by the RIKEN Structural Genomics/Proteomics Initiative (RSGI), the National Project on Protein Structural and Functional Analysis, Ministry of Education, Culture, Sports, Science, and Technology of Japan (to S.Y.).
PY - 2007/3/9
Y1 - 2007/3/9
N2 - 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.
AB - 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.
KW - RNA
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U2 - 10.1016/j.molcel.2007.01.027
DO - 10.1016/j.molcel.2007.01.027
M3 - Article
C2 - 17349960
AN - SCOPUS:33847358277
VL - 25
SP - 751
EP - 764
JO - Molecular Cell
JF - Molecular Cell
SN - 1097-2765
IS - 5
ER -