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-Structure paper
タイトル | Molecular basis for erythromycin-dependent ribosome stalling during translation of the ErmBL leader peptide. |
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ジャーナル・号・ページ | Nat Commun, Vol. 5, Page 3501, Year 2014 |
掲載日 | 2014年3月24日 |
著者 | Stefan Arenz / Haripriya Ramu / Pulkit Gupta / Otto Berninghausen / Roland Beckmann / Nora Vázquez-Laslop / Alexander S Mankin / Daniel N Wilson / |
PubMed 要旨 | 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 ...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. |
リンク | Nat Commun / PubMed:24662426 / PubMed Central |
手法 | EM (単粒子) |
解像度 | 6.6 Å |
構造データ | |
化合物 |
ChemComp-UNL: ChemComp-ERY: |
由来 |
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キーワード | RIBOSOME/ANTIBIOTIC / erythromycin / stalling / RIBOSOME-ANTIBIOTIC complex |