5OT7

Elongation factor G-ribosome complex captures in the absence of inhibitors.

これはPDB形式変換不可エントリーです。

5OT7 の概要

• エントリーDOI: 10.2210/pdb5ot7/pdb
• EMDBエントリー: 3852
• 分子名称: 16S Ribosomal RNA, 30S ribosomal protein S4, 30S ribosomal protein S5, ... (62 entities in total)
• 機能のキーワード: elongation factor g, translation, translocation, ribosome
• 由来する生物種: Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579); 詳細
• 細胞内の位置: Cytoplasm: Q5SHN5
• タンパク質・核酸の鎖数: 59
• 化学式量合計: 2303759.09

構造登録者

Mace, K.,Giudice, E.,Chat, S.,Gillet, R. (登録日: 2017-08-21, 公開日: 2018-02-14, 最終更新日: 2025-10-01)

主引用文献

Mace, K.,Giudice, E.,Chat, S.,Gillet, R.
The structure of an elongation factor G-ribosome complex captured in the absence of inhibitors.
Nucleic Acids Res., 46:3211-3217, 2018

PubMed Abstract: During translation's elongation cycle, elongation factor G (EF-G) promotes messenger and transfer RNA translocation through the ribosome. Until now, the structures reported for EF-G-ribosome complexes have been obtained by trapping EF-G in the ribosome. These results were based on use of non-hydrolyzable guanosine 5'-triphosphate (GTP) analogs, specific inhibitors or a mutated EF-G form. Here, we present the first cryo-electron microscopy structure of EF-G bound to ribosome in the absence of an inhibitor. The structure reveals a natural conformation of EF-G·GDP in the ribosome, with a previously unseen conformation of its third domain. These data show how EF-G must affect translocation, and suggest the molecular mechanism by which fusidic acid antibiotic prevents the release of EF-G after GTP hydrolysis.

PubMed: 29408956
DOI: 10.1093/nar/gky081

実験手法

ELECTRON MICROSCOPY (3.8 Å)