9MTP

Crystal structure of the wild-type Thermus thermophilus 70S ribosome in complex with mRNA, A-site Q230-N5-methylated Release Factor 1, and P-site fMEAAAKC-peptidyl-tRNAcys at 2.40A resolution

これはPDB形式変換不可エントリーです。

9MTP の概要

• エントリーDOI: 10.2210/pdb9mtp/pdb
• 分子名称: 23S Ribosomal RNA, 50S ribosomal protein L14, 50S ribosomal protein L15, ... (61 entities in total)
• 機能のキーワード: translation termination; peptide release; release factor; hydrolysis; peptidyl-trna; non-hydrolyzable; 70s ribosome; x-ray structure; pre-termination state; peptidyl transferase center, ribosome
• 由来する生物種: Thermus thermophilus HB8; 詳細
• タンパク質・核酸の鎖数: 112
• 化学式量合計: 4548845.62

構造登録者

Aleksandrova, E.V.,Syroegin, E.A.,Basu, R.S.,Vassilevski, A.A.,Gagnon, M.G.,Polikanov, Y.S. (登録日: 2025-01-12, 公開日: 2025-06-18, 最終更新日: 2025-07-02)

主引用文献

Aleksandrova, E.V.,Syroegin, E.A.,Basu, R.S.,Vassilevski, A.A.,Gagnon, M.G.,Polikanov, Y.S.
Mechanism of release factor-mediated peptidyl-tRNA hydrolysis on the ribosome.
Science, 388:eads9030-eads9030, 2025

PubMed Abstract: Translation termination is essential in all living organisms because it ensures that proteins have lengths strictly defined by their genes. This universal process is mediated by peptide release factors (RFs) that recognize stop codons and catalyze the hydrolysis of peptidyl transfer RNA (peptidyl-tRNA) on the ribosome, presumably by activating a water molecule. We report structures of the bacterial ribosome in complex with peptidyl-tRNA and RFs in the prepeptide release state. No hydrolytic water molecule was seen in the peptidyl transferase center. Instead, RFs induced rearrangements of the peptidyl-tRNA adenine 76 (A76) ribose pucker that orient the 2'-OH for the nucleophilic attack onto the neighboring carbonyl group. These findings suggest a catalytic mechanism of RF-mediated peptide release and provide a structural basis for the universal conservation of the catalytic domain in peptide RFs.

PubMed: 40536958
DOI: 10.1126/science.ads9030

実験手法

X-RAY DIFFRACTION (2.4 Å)