5O2R

Cryo-EM structure of the proline-rich antimicrobial peptide Api137 bound to the terminating ribosome

これはPDB形式変換不可エントリーです。

5O2R の概要

• エントリーDOI: 10.2210/pdb5o2r/pdb
• EMDBエントリー: 3730
• 分子名称: 23S ribosomal RNA, 50S ribosomal protein L13, 50S ribosomal protein L14, ... (58 entities in total)
• 機能のキーワード: ribosome, termination, release factors, antimicrobial peptides, antibiotic
• 由来する生物種: Escherichia coli K-12; 詳細
• タンパク質・核酸の鎖数: 58
• 化学式量合計: 2196433.95

構造登録者

Graf, M.,Berninghausen, O.,Beckmann, R.,Wilson, D.N. (登録日: 2017-05-22, 公開日: 2017-07-26, 最終更新日: 2024-11-13)

主引用文献

Florin, T.,Maracci, C.,Graf, M.,Karki, P.,Klepacki, D.,Berninghausen, O.,Beckmann, R.,Vazquez-Laslop, N.,Wilson, D.N.,Rodnina, M.V.,Mankin, A.S.
An antimicrobial peptide that inhibits translation by trapping release factors on the ribosome.
Nat. Struct. Mol. Biol., 24:752-757, 2017

PubMed Abstract: Many antibiotics stop bacterial growth by inhibiting different steps of protein synthesis. However, no specific inhibitors of translation termination are known. Proline-rich antimicrobial peptides, a component of the antibacterial defense system of multicellular organisms, interfere with bacterial growth by inhibiting translation. Here we show that Api137, a derivative of the insect-produced antimicrobial peptide apidaecin, arrests terminating ribosomes using a unique mechanism of action. Api137 binds to the Escherichia coli ribosome and traps release factor (RF) RF1 or RF2 subsequent to the release of the nascent polypeptide chain. A high-resolution cryo-EM structure of the ribosome complexed with RF1 and Api137 reveals the molecular interactions that lead to RF trapping. Api137-mediated depletion of the cellular pool of free release factors causes the majority of ribosomes to stall at stop codons before polypeptide release, thereby resulting in a global shutdown of translation termination.

PubMed: 28741611
DOI: 10.1038/nsmb.3439

実験手法

ELECTRON MICROSCOPY (3.4 Å)