6BOH

Antibiotic blasticidin S and E. coli release factor 1 (containing deletion 302-304) bound to the 70S ribosome

これはPDB形式変換不可エントリーです。

6BOH の概要

• エントリーDOI: 10.2210/pdb6boh/pdb
• 分子名称: 16S ribosomal RNA, 50S ribosomal protein L9, 50S ribosomal protein L13, ... (58 entities in total)
• 機能のキーワード: class i release factors, closed rf1, stop-codon recognition, termination accuracy, blasticidin s, ribosome-antibiotic complex, ribosome/antibiotic
• 由来する生物種: Escherichia coli; 詳細
• タンパク質・核酸の鎖数: 114
• 化学式量合計: 4622553.74

構造登録者

Svidritskiy, E.,Korostelev, A.A. (登録日: 2017-11-20, 公開日: 2018-05-23, 最終更新日: 2025-03-19)

主引用文献

Svidritskiy, E.,Korostelev, A.A.
Conformational Control of Translation Termination on the 70S Ribosome.
Structure, 26:821-, 2018

PubMed Abstract: Translation termination ensures proper lengths of cellular proteins. During termination, release factor (RF) recognizes a stop codon and catalyzes peptide release. Conformational changes in RF are thought to underlie accurate translation termination. However, structural studies of ribosome termination complexes have only captured RFs in a conformation that is consistent with the catalytically active state. Here, we employ a hyper-accurate RF1 variant to obtain crystal structures of 70S termination complexes that suggest a structural pathway for RF1 activation. We trapped RF1 conformations with the catalytic domain outside of the peptidyl-transferase center, while the codon-recognition domain binds the stop codon. Stop-codon recognition induces 30S decoding-center rearrangements that precede accommodation of the catalytic domain. The separation of codon recognition from the opening of the catalytic domain suggests how rearrangements in RF1 and in the ribosomal decoding center coordinate stop-codon recognition with peptide release, ensuring accurate translation termination.

PubMed: 29731232
DOI: 10.1016/j.str.2018.04.001

実験手法

X-RAY DIFFRACTION (3.4 Å)