8ANA

Cryo-EM structure of the proline-rich antimicrobial peptide drosocin bound to the 50S ribosomal subunit

8ANA の概要

• エントリーDOI: 10.2210/pdb8ana/pdb
• 関連するPDBエントリー: 8AKN 8AM9
• EMDBエントリー: 15488 15523 15533
• 分子名称: 50S ribosomal protein L33, 50S ribosomal protein L3, 50S ribosomal protein L4, ... (37 entities in total)
• 機能のキーワード: e.coli, drosocin, dro1, antimicrobial peptide, proline-rich, pramp, 50s, ribosome
• 由来する生物種: Escherichia coli BW25113; 詳細
• タンパク質・核酸の鎖数: 32
• 化学式量合計: 1358423.56

構造登録者

Koller, T.O.,Morici, M.,Wilson, D.N. (登録日: 2022-08-05, 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

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

実験手法

ELECTRON MICROSCOPY (2.1 Å)