6OMC

capsid of T5 virion

6OMC の概要

• エントリーDOI: 10.2210/pdb6omc/pdb
• EMDBエントリー: 20099 20122 20123 20125
• 分子名称: Major capsid protein (1 entity in total)
• 機能のキーワード: capsid, hk97-fold, dsdna-phage, icosahedral, virus
• 由来する生物種: Escherichia phage T5
• タンパク質・核酸の鎖数: 13
• 化学式量合計: 428107.67

構造登録者

Huet, A.,Duda, R.L.,Boulanger, P.,Conway, J.F. (登録日: 2019-04-18, 公開日: 2019-10-02, 最終更新日: 2024-03-20)

主引用文献

Huet, A.,Duda, R.L.,Boulanger, P.,Conway, J.F.
Capsid expansion of bacteriophage T5 revealed by high resolution cryoelectron microscopy.
Proc.Natl.Acad.Sci.USA, 116:21037-21046, 2019

PubMed Abstract: The large (90-nm) icosahedral capsid of bacteriophage T5 is composed of 775 copies of the major capsid protein (mcp) together with portal, protease, and decoration proteins. Its assembly is a regulated process that involves several intermediates, including a thick-walled round precursor prohead that expands as the viral DNA is packaged to yield a thin-walled and angular mature capsid. We investigated capsid maturation by comparing cryoelectron microscopy (cryo-EM) structures of the prohead, the empty expanded capsid both with and without decoration protein, and the virion capsid at a resolution of 3.8 Å for the latter. We detail the molecular structure of the mcp, its complex pattern of interactions, and their evolution during maturation. The bacteriophage T5 mcp is a variant of the canonical HK97-fold with a high level of plasticity that allows for the precise assembly of a giant macromolecule and the adaptability needed to interact with other proteins and the packaged DNA.

PubMed: 31578255
DOI: 10.1073/pnas.1909645116

実験手法

ELECTRON MICROSCOPY (3.8 Å)