9B40

Pseudomonas phage Pa193 5-fold vertex (capsid, decorating, and scaffolding proteins)

これはPDB形式変換不可エントリーです。

9B40 の概要

• エントリーDOI: 10.2210/pdb9b40/pdb
• EMDBエントリー: 44163
• 分子名称: gp26 Major capsid, gp25 Decorating protein, gp24 Scaffolding protein (3 entities in total)
• 機能のキーワード: phage, bacteriophage, gene product 24 (gp24), structural protein, viral protein, gene product 25 (gp25), scaffolding protein, decorating protein, major capsid protein, gene product 26 (gp26)
• 由来する生物種: Pseudomonas virus Pa193; 詳細
• タンパク質・核酸の鎖数: 19
• 化学式量合計: 782292.49

構造登録者

Iglesias, S.M.,Cingolani, G. (登録日: 2024-03-20, 公開日: 2024-10-16)

主引用文献

Iglesias, S.M.,Hou, C.D.,Reid, J.,Schauer, E.,Geier, R.,Soriaga, A.,Sim, L.,Gao, L.,Whitelegge, J.,Kyme, P.,Birx, D.,Lemire, S.,Cingolani, G.
Cryo-EM analysis of Pseudomonas phage Pa193 structural components.
Commun Biol, 7:1275-1275, 2024

PubMed Abstract: The World Health Organization has designated Pseudomonas aeruginosa as a critical pathogen for the development of new antimicrobials. Bacterial viruses, or bacteriophages, have been used in various clinical settings, commonly called phage therapy, to address this growing public health crisis. Here, we describe a high-resolution structural atlas of a therapeutic, contractile-tailed Pseudomonas phage, Pa193. We used bioinformatics, proteomics, and cryogenic electron microscopy single particle analysis to identify, annotate, and build atomic models for 21 distinct structural polypeptide chains forming the icosahedral capsid, neck, contractile tail, and baseplate. We identified a putative scaffolding protein stabilizing the interior of the capsid 5-fold vertex. We also visualized a large portion of Pa193 ~ 500 Å long tail fibers and resolved the interface between the baseplate and tail fibers. The work presented here provides a framework to support a better understanding of phages as biomedicines for phage therapy and inform engineering opportunities.

PubMed: 39370451
DOI: 10.1038/s42003-024-06985-x

実験手法

ELECTRON MICROSCOPY (2.9 Å)