Loading
PDBj
メニューPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

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DOI10.2210/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_IDPRD_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
Koller, T.O.,Morici, M.,Wilson, D.N. (登録日: 2022-08-03, 公開日: 2023-03-08, 最終更新日: 2025-03-12)
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: 36997646
DOI: 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)
構造検証レポート
Validation report summary of 8am9
検証レポート(詳細版)ダウンロードをダウンロード

246905

件を2025-12-31に公開中

PDB statisticsPDBj update infoContact PDBjnumon