8H89

Capsid of Ralstonia phage GP4

8H89 の概要

• エントリーDOI: 10.2210/pdb8h89/pdb
• EMDBエントリー: 34539
• 分子名称: Major capsid protein, Virion associated protein (2 entities in total)
• 機能のキーワード: ralstonia phage gp4, complex, virus
• 由来する生物種: Ralstonia phage GP4; 詳細
• タンパク質・核酸の鎖数: 18
• 化学式量合計: 509755.36

構造登録者

Liu, H.R.,Chen, W.Y. (登録日: 2022-10-22, 公開日: 2022-11-16, 最終更新日: 2023-08-30)

主引用文献

Zheng, J.,Chen, W.,Xiao, H.,Yang, F.,Li, X.,Song, J.,Cheng, L.,Liu, H.
A Capsid Structure of Ralstonia solanacearum podoviridae GP4 with a Triangulation Number T = 9.
Viruses, 14:-, 2022

PubMed Abstract: GP4, a new phage, is a short-tailed phage. Few structures of phages have been resolved to near-atomic resolution until now. Here, we present a 3.7 Å resolution structure of the GP4 head by cryo-electron microscopy (cryo-EM). The GP4 head contains 540 copies of major capsid protein (MCP) gp2 and 540 copies of cement protein (CP) gp1 arranged in an icosahedral shell with a triangulation number T = 9. The structures of gp2 and gp1 show a canonical HK97-like fold and an Ig-like fold, respectively. The trimeric CPs stick on the surface of the head along the quasi-threefold axis of the icosahedron generating a sandwiched three-layer electrostatic complementary potential, thereby enhancing the head stability. The assembly pattern of the GP4 head provides a platform for the further exploration of the interaction between and corresponding phages.

PubMed: 36366529
DOI: 10.3390/v14112431

実験手法

ELECTRON MICROSCOPY (3.7 Å)