4CTF

The limits of structural plasticity in a picornavirus capsid revealed by a massively expanded equine rhinitis A virus particle

これはPDB形式変換不可エントリーです。

4CTF の概要

• エントリーDOI: 10.2210/pdb4ctf/pdb
• EMDBエントリー: 2389
• 分子名称: VP1, EQUINE RHINITIS A VIRUS, P1, ... (4 entities in total)
• 機能のキーワード: virus, picornavirus, capsid structure, capsid expansion, uncoating
• 由来する生物種: EQUINE RHINITIS A VIRUS; 詳細
• タンパク質・核酸の鎖数: 240
• 化学式量合計: 5102611.20

構造登録者

Bakker, S.E.,Groppelli, E.,Pearson, A.R.,Stockley, P.G.,Rowlands, D.J.,Ranson, N.A. (登録日: 2014-03-13, 公開日: 2014-05-21, 最終更新日: 2024-05-08)

主引用文献

Bakker, S.E.,Groppelli, E.,Pearson, A.R.,Stockley, P.G.,Rowlands, D.J.,Ranson, N.A.
Limits of Structural Plasticity in a Picornavirus Capsid Revealed by a Massively Expanded Equine Rhinitis a Virus Particle.
J.Virol., 88:6093-, 2014

PubMed Abstract: The Picornaviridae family of small, nonenveloped viruses includes major pathogens of humans and animals. They have positive-sense, single-stranded RNA genomes, and the mechanism(s) by which these genomes are introduced into cells to initiate infection remains poorly understood. The structures of presumed uncoating intermediate particles of several picornaviruses show limited expansion and some increased porosity compared to the mature virions. Here, we present the cryo-electron microscopy structure of native equine rhinitis A virus (ERAV), together with the structure of a massively expanded ERAV particle, each at ∼17-Å resolution. The expanded structure has large pores on the particle 3-fold axes and has lost the RNA genome and the capsid protein VP4. The expanded structure thus illustrates both the limits of structural plasticity in such capsids and a plausible route by which genomic RNA might exit.

PubMed: 24648455
DOI: 10.1128/JVI.01979-13

実験手法

ELECTRON MICROSCOPY (17 Å)