5JTE

Cryo-EM structure of an ErmBL-stalled ribosome in complex with A-, P-, and E-tRNA

これはPDB形式変換不可エントリーです。

5JTE の概要

• エントリーDOI: 10.2210/pdb5jte/pdb
• EMDBエントリー: 8175
• 分子名称: 16S ribosomal RNA, 30S ribosomal protein S10, 30S ribosomal protein S11, ... (59 entities in total)
• 機能のキーワード: ribosome, ermbl, stalling, translation, erythromycin
• 由来する生物種: Escherichia coli; 詳細
• タンパク質・核酸の鎖数: 57
• 化学式量合計: 2221174.83

構造登録者

Arenz, S.,Bock, L.V.,Graf, M.,Innis, C.A.,Beckmann, R.,Grubmueller, H.,Vaiana, A.C.,Wilson, D.N. (登録日: 2016-05-09, 公開日: 2016-07-20, 最終更新日: 2024-10-16)

主引用文献

Arenz, S.,Bock, L.V.,Graf, M.,Innis, C.A.,Beckmann, R.,Grubmuller, H.,Vaiana, A.C.,Wilson, D.N.
A combined cryo-EM and molecular dynamics approach reveals the mechanism of ErmBL-mediated translation arrest.
Nat Commun, 7:12026-12026, 2016

PubMed Abstract: Nascent polypeptides can induce ribosome stalling, regulating downstream genes. Stalling of ErmBL peptide translation in the presence of the macrolide antibiotic erythromycin leads to resistance in Streptococcus sanguis. To reveal this stalling mechanism we obtained 3.6-Å-resolution cryo-EM structures of ErmBL-stalled ribosomes with erythromycin. The nascent peptide adopts an unusual conformation with the C-terminal Asp10 side chain in a previously unseen rotated position. Together with molecular dynamics simulations, the structures indicate that peptide-bond formation is inhibited by displacement of the peptidyl-tRNA A76 ribose from its canonical position, and by non-productive interactions of the A-tRNA Lys11 side chain with the A-site crevice. These two effects combine to perturb peptide-bond formation by increasing the distance between the attacking Lys11 amine and the Asp10 carbonyl carbon. The interplay between drug, peptide and ribosome uncovered here also provides insight into the fundamental mechanism of peptide-bond formation.

PubMed: 27380950
DOI: 10.1038/ncomms12026

実験手法

ELECTRON MICROSCOPY (3.6 Å)