7F2P

The head structure of Helicobacter pylori bacteriophage KHP40

7F2P の概要

• エントリーDOI: 10.2210/pdb7f2p/pdb
• EMDBエントリー: 30778 30800
• 分子名称: Cement protein gp16, KHP40 MCP (2 entities in total)
• 機能のキーワード: capsid, phage, phage head, cryoem, virus
• 由来する生物種: Helicobacter phage KHP40; 詳細
• タンパク質・核酸の鎖数: 18
• 化学式量合計: 506923.45

構造登録者

Kamiya, R.,Uchiyama, J.,Matsuzaki, S.,Murata, K.,Iwasaki, K.,Miyazaki, N. (登録日: 2021-06-13, 公開日: 2021-10-27, 最終更新日: 2025-07-02)

主引用文献

Kamiya, R.,Uchiyama, J.,Matsuzaki, S.,Murata, K.,Iwasaki, K.,Miyazaki, N.
Acid-stable capsid structure of Helicobacter pylori bacteriophage KHP30 by single-particle cryoelectron microscopy.
Structure, 30:300-, 2022

PubMed Abstract: The acid-stable capsid structures of Helicobacter pylori phages KHP30 and KHP40 are solved at 2.7 and 3.0 Å resolutions by cryoelectron microscopy, respectively. The capsids have icosahedral T = 9 symmetry and consist of each 540 copies of 2 structural proteins, a major capsid protein, and a cement protein. The major capsid proteins form 12 pentagonal capsomeres occupying icosahedral vertexes and 80 hexagonal capsomeres located at icosahedral faces and edges. The major capsid protein has a unique protruding loop extending to the neighboring subunit that stabilizes hexagonal capsomeres. Furthermore, the capsid is decorated with trimeric cement proteins with a jelly roll motif. The cement protein trimer sits on the quasi-three-fold axis formed by three major capsid protein capsomeres, thereby enhancing the particle stability by connecting these capsomeres. Sequence and structure comparisons between the related Helicobacter pylori phages suggest a possible mechanism of phage adaptation to the human gastric environment.

PubMed: 34597601
DOI: 10.1016/j.str.2021.09.001

実験手法

ELECTRON MICROSCOPY (3 Å)