8AM9
Cryo-EM structure of the proline-rich antimicrobial peptide drosocin bound to the elongating ribosome
これはPDB形式変換不可エントリーです。
8AM9 の概要
| エントリーDOI | 10.2210/pdb8am9/pdb |
| 関連するPDBエントリー | 8AKN |
| EMDBエントリー | 15488 15523 |
| 関連するBIRD辞書のPRD_ID | PRD_002425 |
| 分子名称 | 50S ribosomal protein L33, 30S ribosomal protein S5, 30S ribosomal protein S6, fully modified isoform, ... (61 entities in total) |
| 機能のキーワード | e.coli, 70s, drosocin, dro1, antimicrobial peptide, proline-rich, pramp, initiator trna, elongation, ribosome, leucine trna |
| 由来する生物種 | Drosophila melanogaster (fruit fly) 詳細 |
| タンパク質・核酸の鎖数 | 56 |
| 化学式量合計 | 2203313.42 |
| 構造登録者 | |
| 主引用文献 | Koller, T.O.,Morici, M.,Berger, M.,Safdari, H.A.,Lele, D.S.,Beckert, B.,Kaur, K.J.,Wilson, D.N. Structural basis for translation inhibition by the glycosylated drosocin peptide. Nat.Chem.Biol., 19:1072-1081, 2023 Cited by PubMed Abstract: The proline-rich antimicrobial peptide (PrAMP) drosocin is produced by Drosophila species to combat bacterial infection. Unlike many PrAMPs, drosocin is O-glycosylated at threonine 11, a post-translation modification that enhances its antimicrobial activity. Here we demonstrate that the O-glycosylation not only influences cellular uptake of the peptide but also interacts with its intracellular target, the ribosome. Cryogenic electron microscopy structures of glycosylated drosocin on the ribosome at 2.0-2.8-Å resolution reveal that the peptide interferes with translation termination by binding within the polypeptide exit tunnel and trapping RF1 on the ribosome, reminiscent of that reported for the PrAMP apidaecin. The glycosylation of drosocin enables multiple interactions with U2609 of the 23S rRNA, leading to conformational changes that break the canonical base pair with A752. Collectively, our study reveals novel molecular insights into the interaction of O-glycosylated drosocin with the ribosome, which provide a structural basis for future development of this class of antimicrobials. PubMed: 36997646DOI: 10.1038/s41589-023-01293-7 主引用文献が同じPDBエントリー |
| 実験手法 | ELECTRON MICROSCOPY (2.8 Å) |
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