A structural dendrogram of the actinobacteriophage major capsid proteins provides important structural insights into the evolution of capsid stability

被引：11

作者：

Podgorski, Jennifer M. ^{[1
]}

Freeman, Krista ^{[2
]}

Gosselin, Sophia ^{[1
]}

Huet, Alexis ^{[3
]}

Conway, James F. ^{[3
]}

Bird, Mary ^{[1
]}

Grecco, John ^{[1
]}

Patel, Shreya ^{[1
]}

Jacobs-Sera, Deborah ^{[2
]}

Hatfull, Graham ^{[2
]}

Gogarten, Johann Peter ^{[1
,4
]}

Ravantti, Janne ^{[5
]}

White, Simon J. ^{[1
]}

机构：

[1] Univ Connecticut, Dept Mol & Cell Biol, Biol Phys Bldg, 91 North Eagleville Rd,Unit 3125, Storrs, CT 06269 USA

[2] Univ Pittsburgh, Dept Biol Sci, Clapp Hall,4249 Fifth Ave, Pittsburgh, PA 15260 USA

[3] Univ Pittsburgh, Sch Med, Dept Struct Biol, Pittsburgh, PA USA

[4] Univ Connecticut, Inst Syst Genom, Storrs, CT 06268 USA

[5] Univ Helsinki, Mol & Integrat Biosci Res Programme, Helsinki, Finland

来源：

STRUCTURE | 2023年 / 31卷 / 03期

基金：

美国国家卫生研究院;

关键词：

CRYO-EM; ANGSTROM RESOLUTION; COAT PROTEIN; PHAGE; DNA; MECHANISM; GENOME; EJECTION; DOMAIN; VIRUS;

D O I：

10.1016/j.str.2022.12.012

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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 stabiliza-tion 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 compar-isons, phylogenetic analyses, and Alphafold predictions, we have constructed a detailed structural dendro-gram 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.

引用

页码：282 / +

页数：19

共 83 条

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