3J5L

Structure of the E. coli 50S subunit with ErmBL nascent chain

3J5L の概要

• エントリーDOI: 10.2210/pdb3j5l/pdb
• EMDBエントリー: 5771
• 分子名称: 50S ribosomal protein L32, 5S ribosomal RNA, 50S ribosomal protein L2, ... (36 entities in total)
• 機能のキーワード: erythromycin, stalling, 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: 34
• 化学式量合計: 1345995.94

構造登録者

Arenz, S.,Ramu, H.,Gupta, P.,Berninghausen, O.,Beckmann, R.,Vazquez-Laslop, N.,Mankin, A.S.,Wilson, D.N. (登録日: 2013-10-23, 公開日: 2014-03-26, 最終更新日: 2024-11-06)

主引用文献

Arenz, S.,Ramu, H.,Gupta, P.,Berninghausen, O.,Beckmann, R.,Vazquez-Laslop, N.,Mankin, A.S.,Wilson, D.N.
Molecular basis for erythromycin-dependent ribosome stalling during translation of the ErmBL leader peptide.
Nat Commun, 5:3501-3501, 2014

PubMed Abstract: In bacteria, ribosome stalling during translation of ErmBL leader peptide occurs in the presence of the antibiotic erythromycin and leads to induction of expression of the downstream macrolide resistance methyltransferase ErmB. The lack of structures of drug-dependent stalled ribosome complexes (SRCs) has limited our mechanistic understanding of this regulatory process. Here we present a cryo-electron microscopy structure of the erythromycin-dependent ErmBL-SRC. The structure reveals that the antibiotic does not interact directly with ErmBL, but rather redirects the path of the peptide within the tunnel. Furthermore, we identify a key peptide-ribosome interaction that defines an important relay pathway from the ribosomal tunnel to the peptidyltransferase centre (PTC). The PTC of the ErmBL-SRC appears to adopt an uninduced state that prevents accommodation of Lys-tRNA at the A-site, thus providing structural basis for understanding how the drug and the nascent peptide cooperate to inhibit peptide bond formation and induce translation arrest.

PubMed: 24662426
DOI: 10.1038/ncomms4501

実験手法

ELECTRON MICROSCOPY (6.6 Å)