2OM7

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

2OM7 の概要

• エントリーDOI: 10.2210/pdb2om7/pdb
• 関連するPDBエントリー: 1FNM 1WDT 1YL3 1YL4 2j00 2j01
• EMDBエントリー: 1315
• 分子名称: Fragment of 16S rRNA (h14), p/E-tRNA, 30S ribosomal protein S12, ... (14 entities in total)
• 機能のキーワード: rna-protein complex, ribosome
• 由来する生物種: Thermus thermophilus; 詳細
• タンパク質・核酸の鎖数: 14
• 化学式量合計: 404602.11

構造登録者

Connell, S.R.,Wilson, D.N.,Rost, M.,Schueler, M.,Giesebrecht, J.,Dabrowski, M.,Mielke, T.,Fucini, P.,Spahn, C.M.T. (登録日: 2007-01-21, 公開日: 2008-01-15, 最終更新日: 2023-12-27)

主引用文献

Connell, S.R.,Takemoto, C.,Wilson, D.N.,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.
Structural basis for interaction of the ribosome with the switch regions of GTP-bound elongation factors.
Mol.Cell, 25:751-764, 2007

PubMed 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.

PubMed: 17349960
DOI: 10.1016/j.molcel.2007.01.027

実験手法

ELECTRON MICROSCOPY (7.3 Å)