8ECJ

Mycobacterium phage Cain

8ECJ の概要

• エントリーDOI: 10.2210/pdb8ecj/pdb
• EMDBエントリー: 28016 28017 28018 28020 28021
• 分子名称: Major capsid protein (1 entity in total)
• 機能のキーワード: hk97-fold, t=9, tailed bacteriophage, virus
• 由来する生物種: Mycobacterium phage Cain
• タンパク質・核酸の鎖数: 9
• 化学式量合計: 287028.02

構造登録者

Podgorski, J.M.,White, S.J. (登録日: 2022-09-02, 公開日: 2023-02-01, 最終更新日: 2024-06-19)

主引用文献

Podgorski, J.M.,Freeman, K.,Gosselin, S.,Huet, A.,Conway, J.F.,Bird, M.,Grecco, J.,Patel, S.,Jacobs-Sera, D.,Hatfull, G.,Gogarten, J.P.,Ravantti, J.,White, S.J.
A structural dendrogram of the actinobacteriophage major capsid proteins provides important structural insights into the evolution of capsid stability.
Structure, 31:282-, 2023

PubMed Abstract: Many double-stranded DNA viruses, including tailed bacteriophages (phages) and herpesviruses, use the HK97-fold in their major capsid protein to make the capsomers of the icosahedral viral capsid. After the genome packaging at near-crystalline densities, the capsid is subjected to a major expansion and stabilization step that allows it to withstand environmental stresses and internal high pressure. Several different mechanisms for stabilizing the capsid have been structurally characterized, but how these mechanisms have evolved is still not understood. Using cryo-EM structure determination of 10 capsids, structural comparisons, phylogenetic analyses, and Alphafold predictions, we have constructed a detailed structural dendrogram describing the evolution of capsid structural stability within the actinobacteriophages. We show that the actinobacteriophage major capsid proteins can be classified into 15 groups based upon their HK97-fold.

PubMed: 36649709
DOI: 10.1016/j.str.2022.12.012

実験手法

ELECTRON MICROSCOPY (2.9 Å)