8I1V

The asymmetric unit of P22 procapsid

8I1V の概要

• エントリーDOI: 10.2210/pdb8i1v/pdb
• EMDBエントリー: 35123
• 分子名称: Major capsid protein, Scaffolding protein (2 entities in total)
• 機能のキーワード: complex, virus, viral protein
• 由来する生物種: Salmonella phage P22; 詳細
• タンパク質・核酸の鎖数: 14
• 化学式量合計: 562836.06

構造登録者

Xiao, H.,Liu, H.R.,Cheng, L.P. (登録日: 2023-01-13, 公開日: 2023-03-08, 最終更新日: 2025-06-18)

主引用文献

Xiao, H.,Zhou, J.,Yang, F.,Liu, Z.,Song, J.,Chen, W.,Liu, H.,Cheng, L.
Assembly and Capsid Expansion Mechanism of Bacteriophage P22 Revealed by High-Resolution Cryo-EM Structures.
Viruses, 15:-, 2023

PubMed Abstract: The formation of many double-stranded DNA viruses, such as herpesviruses and bacteriophages, begins with the scaffolding-protein-mediated assembly of the procapsid. Subsequently, the procapsid undergoes extensive structural rearrangement and expansion to become the mature capsid. Bacteriophage P22 is an established model system used to study virus maturation. Here, we report the cryo-electron microscopy structures of procapsid, empty procapsid, empty mature capsid, and mature capsid of phage P22 at resolutions of 2.6 Å, 3.9 Å, 2.8 Å, and 3.0 Å, respectively. The structure of the procapsid allowed us to build an accurate model of the coat protein gp5 and the C-terminal region of the scaffolding protein gp8. In addition, interactions among the gp5 subunits responsible for procapsid assembly and stabilization were identified. Two C-terminal α-helices of gp8 were observed to interact with the coat protein in the procapsid. The amino acid interactions between gp5 and gp8 in the procapsid were consistent with the results of previous biochemical studies involving mutant proteins. Our structures reveal hydrogen bonds and salt bridges between the gp5 subunits in the procapsid and the conformational changes of the gp5 domains involved in the closure of the local sixfold opening and a thinner capsid shell during capsid maturation.

PubMed: 36851569
DOI: 10.3390/v15020355

実験手法

ELECTRON MICROSCOPY (2.6 Å)