6C4H

Conformation of methylated GGQ in the peptidyl transferase center during translation termination (PTC region)

6C4H の概要

• エントリーDOI: 10.2210/pdb6c4h/pdb
• EMDBエントリー: 7340 7341
• 分子名称: 23S rRNA, 50S ribosomal protein L2, 50S ribosomal protein L3, ... (8 entities in total)
• 機能のキーワード: nonstop, termination, arfa, rf2, methylation, ribosomal protein-rna complex, ribosomal protein/rna
• 由来する生物種: Escherichia coli; 詳細
• タンパク質・核酸の鎖数: 7
• 化学式量合計: 1087476.69

構造登録者

Zeng, F.,Jin, H. (登録日: 2018-01-12, 公開日: 2018-02-21, 最終更新日: 2024-11-13)

主引用文献

Zeng, F.,Jin, H.
Conformation of methylated GGQ in the Peptidyl Transferase Center during Translation Termination.
Sci Rep, 8:2349-2349, 2018

PubMed Abstract: The universally conserved Gly-Gly-Gln (GGQ) tripeptide in release factors or release factor-like surveillance proteins is required to catalyze the release of nascent peptide in the ribosome. The glutamine of the GGQ is methylated post-translationally at the N position in vivo; this covalent modification is essential for optimal cell growth and efficient translation termination. However, the precise conformation of the methylated-GGQ tripeptide in the ribosome remains unknown. Using cryoEM and X-ray crystallography, we report the conformation of methylated-GGQ in the peptidyl transferase center of the ribosome during canonical translational termination and co-translation quality control. It has been suggested that the GGQ motif arose independently through convergent evolution among otherwise unrelated proteins that catalyze peptide release. The requirement for this tripeptide in the highly conserved peptidyl transferase center suggests that the conformation reported here is likely shared during termination of protein synthesis in all domains of life.

PubMed: 29403017
DOI: 10.1038/s41598-018-20107-8

実験手法

ELECTRON MICROSCOPY (3.1 Å)