9KMG

Cryo-EM Structure of Bacteriophage FCWL1 Capsid

9KMG の概要

• エントリーDOI: 10.2210/pdb9kmg/pdb
• EMDBエントリー: 62429
• 分子名称: Major capsid protein, Decoration protein (2 entities in total)
• 機能のキーワード: t1-like phage, capsid, icosahedrally averaged, virus
• 由来する生物種: Escherichia phage FCWL1; 詳細
• タンパク質・核酸の鎖数: 14
• 化学式量合計: 366264.57

構造登録者

Cai, C.,Wang, Y.,Liu, Y.,Shao, Q.,Wang, A.,Fang, Q. (登録日: 2024-11-16, 公開日: 2025-01-22, 最終更新日: 2025-07-02)

主引用文献

Cai, C.,Wang, Y.,Liu, Y.,Shao, Q.,Wang, A.,Li, L.,Zheng, Y.,Zhang, T.,Luo, Z.,Yang, C.,Fang, Q.
Structures of a T1-like siphophage reveal capsid stabilization mechanisms and high structural similarities with a myophage.
Structure, 33:663-676.e2, 2025

PubMed Abstract: Bacteriophage T1, a member of Siphoviruses, infects Escherichia coli with high efficiency, making it a promising candidate for phage therapy. Here, we report the near-atomic structures of FCWL1, a T1-like phage that belongs to the T1 phage family. We focus on the head, the head-to-tail interface, and its surrounding components. The hexameric capsomer displays unique gaps between neighboring A domains of the major capsid proteins. These gaps are partially filled by the N-loop of the decoration protein, which adopts a unique conformation. These structural features suggest that the phage might employ a novel strategy for stabilizing its head. Furthermore, despite being a siphophage, the head and head-to-tail connector of the phage show high structural similarity to those of a myophage. These findings enhance our understanding of the structure, capsid stabilization mechanism, and evolution of phages in the T1 family.

PubMed: 39914381
DOI: 10.1016/j.str.2025.01.012

実験手法

ELECTRON MICROSCOPY (3.1 Å)