9IN6

Capsid of Vibrio cholerae phage mature VP1

9IN6 の概要

• エントリーDOI: 10.2210/pdb9in6/pdb
• EMDBエントリー: 60702
• 分子名称: major capsid of VP1, SHP of VP1 (2 entities in total)
• 機能のキーワード: phage, virus, vibrio cholera phage, viral protein
• 由来する生物種: Vibrio cholerae; 詳細
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 319007.39

構造登録者

Liu, H.R.,Pang, H. (登録日: 2024-07-05, 公開日: 2024-08-14, 最終更新日: 2025-06-25)

主引用文献

Pang, H.,Fan, F.,Zheng, J.,Xiao, H.,Tan, Z.,Song, J.,Kan, B.,Liu, H.
Three-dimensional structures of Vibrio cholerae typing podophage VP1 in two states.
Structure, 32:2364-2374.e2, 2024

PubMed Abstract: Lytic podophages (VP1-VP5) play crucial roles in subtyping Vibrio cholerae O1 biotype El Tor. However, until now no structures of these phages have been available, which hindered our understanding of the molecular mechanisms of infection and DNA release. Here, we determined the cryoelectron microscopy (cryo-EM) structures of mature and DNA-ejected VP1 structures at near-atomic and subnanometer resolutions, respectively. The VP1 head is composed of 415 copies of the major capsid protein gp7 and 11 turret-shaped spikes. The VP1 tail consists of an adapter, a nozzle, a slender ring, and a tail needle, and is flanked by three extended fibers I and six trimeric fibers II. Conformational changes of fiber II in DNA-ejected VP1 may cause the release of the tail needle and core proteins, forming an elongated tail channel. Our structures provide insights into the molecular mechanisms of infection and DNA release for podophages with a tail needle.

PubMed: 39471801
DOI: 10.1016/j.str.2024.10.005

実験手法

ELECTRON MICROSCOPY (2.8 Å)