31EU

C. difficile phage phiCD508 tail sheath in spontaneously contracted state

31EU の概要

• エントリーDOI: 10.2210/pdb31eu/pdb
• 関連するPDBエントリー: 31ES
• EMDBエントリー: 58348
• 分子名称: gp55 - Tail sheath protein (1 entity in total)
• 機能のキーワード: bacteriophage, phage tail, myophage, contractile injection system, s-layer, virus, helical assembly
• 由来する生物種: Clostridioides difficile
• タンパク質・核酸の鎖数: 18
• 化学式量合計: 954301.72

構造登録者

Bullough, P.A.,Wilson, J.S.,Berry, H.L.,Fagan, R.P. (登録日: 2026-05-31, 公開日: 2026-07-08)

主引用文献

Bullough, P.A.,Wilson, J.S.,Berry, H.L.,Fagan, R.P.
How cryoEM has advanced our understanding of bacteriophages and bacteriocins targeting Clostridioides difficile.
Iucrj, 2026

PubMed Abstract: We review the structural and functional characteristics of bacteriophages and bacteriocins (diffocins) that specifically target Clostridioides difficile, a significant healthcare concern due to its role in nosocomial infections. The advent of modern cryogenic electron microscopy (cryoEM) has revolutionized our understanding of these contractile injection systems, providing high-resolution insights into their mechanisms. We compare the structures of C. difficile phages and diffocins, highlighting their adaptations for penetrating the Gram-positive bacterial cell envelope - including the cell membrane, cell wall and proteinaceous surface layer. Diffocins, simpler in structure, utilize a combination of mechanical and enzymatic strategies, while some phages like ΦCD508 may rely on mechanical force alone. This review delves into the assembly and function of key components such as the contractile sheath, baseplate and receptor-binding proteins, offering a framework for engineering precision antimicrobials. We also present new experimental results, including refined cryoEM structures of the ΦCD508 pre- and post-contracted tail, a novel spontaneously contracted conformation and an X-ray crystal structure of a phage receptor-binding protein domain. This work underscores the potential of cryoEM in advancing our understanding of phage biology and its applications in developing targeted therapies against C. difficile.

PubMed: 42334192
DOI: 10.1107/S2052252526005105

実験手法

ELECTRON MICROSCOPY (4.3 Å)