1JQS

Fitting of L11 protein and elongation factor G (domain G' and V) in the cryo-em map of E. coli 70S ribosome bound with EF-G and GMPPCP, a nonhydrolysable GTP analog

1JQS の概要

• エントリーDOI: 10.2210/pdb1jqs/pdb
• 関連するPDBエントリー: 1EG0
• 分子名称: 50S Ribosomal protein L11, Elongation Factor G (3 entities in total)
• 機能のキーワード: l11, ef-g, cryo-em, 70s e.coli ribosome, gtp state, ribosome
• 由来する生物種: Escherichia coli; 詳細
• 細胞内の位置: Cytoplasm: P13551 P13551
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 26102.42

構造登録者

Agrawal, R.K.,Linde, J.,Segupta, J.,Nierhaus, K.H.,Frank, J. (登録日: 2001-08-07, 公開日: 2001-09-07, 最終更新日: 2024-02-07)

主引用文献

Agrawal, R.K.,Linde, J.,Sengupta, J.,Nierhaus, K.H.,Frank, J.
Localization of L11 protein on the ribosome and elucidation of its involvement in EF-G-dependent translocation.
J.Mol.Biol., 311:777-787, 2001

PubMed Abstract: L11 protein is located at the base of the L7/L12 stalk of the 50 S subunit of the Escherichia coli ribosome. Because of the flexible nature of the region, recent X-ray crystallographic studies of the 50 S subunit failed to locate the N-terminal domain of the protein. We have determined the position of the complete L11 protein by comparing a three-dimensional cryo-EM reconstruction of the 70 S ribosome, isolated from a mutant lacking ribosomal protein L11, with the three-dimensional map of the wild-type ribosome. Fitting of the X-ray coordinates of L11-23 S RNA complex and EF-G into the cryo-EM maps combined with molecular modeling, reveals that, following EF-G-dependent GTP hydrolysis, domain V of EF-G intrudes into the cleft between the 23 S ribosomal RNA and the N-terminal domain of L11 (where the antibiotic thiostrepton binds), causing the N-terminal domain to move and thereby inducing the formation of the arc-like connection with the G' domain of EF-G. The results provide a new insight into the mechanism of EF-G-dependent translocation.

PubMed: 11518530
DOI: 10.1006/jmbi.2001.4907

実験手法

ELECTRON MICROSCOPY (18 Å)