7OTC
Cryo-EM structure of an Escherichia coli 70S ribosome in complex with elongation factor G and the antibiotic Argyrin B
これはPDB形式変換不可エントリーです。
7OTC の概要
エントリーDOI | 10.2210/pdb7otc/pdb |
関連するPDBエントリー | 7UG7 |
EMDBエントリー | 13058 26486 |
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 | antibiotic, ribosome, translation |
由来する生物種 | Escherichia coli BL21(DE3) 詳細 |
タンパク質・核酸の鎖数 | 52 |
化学式量合計 | 2188658.26 |
構造登録者 | |
主引用文献 | Wieland, M.,Holm, M.,Rundlet, E.J.,Morici, M.,Koller, T.O.,Maviza, T.P.,Pogorevc, D.,Osterman, I.A.,Muller, R.,Blanchard, S.C.,Wilson, D.N. The cyclic octapeptide antibiotic argyrin B inhibits translation by trapping EF-G on the ribosome during translocation. Proc.Natl.Acad.Sci.USA, 119:e2114214119-e2114214119, 2022 Cited by PubMed Abstract: Argyrins are a family of naturally produced octapeptides that display promising antimicrobial activity against Pseudomonas aeruginosa. Argyrin B (ArgB) has been shown to interact with an elongated form of the translation elongation factor G (EF-G), leading to the suggestion that argyrins inhibit protein synthesis by interfering with EF-G binding to the ribosome. Here, using a combination of cryo-electron microscopy (cryo-EM) and single-molecule fluorescence resonance energy transfer (smFRET), we demonstrate that rather than interfering with ribosome binding, ArgB rapidly and specifically binds EF-G on the ribosome to inhibit intermediate steps of the translocation mechanism. Our data support that ArgB inhibits conformational changes within EF-G after GTP hydrolysis required for translocation and factor dissociation, analogous to the mechanism of fusidic acid, a chemically distinct antibiotic that binds a different region of EF-G. These findings shed light on the mechanism of action of the argyrin-class antibiotics on protein synthesis as well as the nature and importance of rate-limiting, intramolecular conformational events within the EF-G-bound ribosome during late-steps of translocation. PubMed: 35500116DOI: 10.1073/pnas.2114214119 主引用文献が同じPDBエントリー |
実験手法 | ELECTRON MICROSCOPY (2.9 Å) |
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