1NO7

Structure of the Large Protease Resistant Upper Domain of VP5, the Major Capsid Protein of Herpes Simplex Virus-1

1NO7 の概要

• エントリーDOI: 10.2210/pdb1no7/pdb
• 分子名称: Major capsid protein (1 entity in total)
• 機能のキーワード: novel fold, alpha plus beta, viral capsid protein, folding nucleus, viral protein
• 由来する生物種: Human herpesvirus 1 (Herpes simplex virus type 1)
• 細胞内の位置: Virion: P06491
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 130339.53

構造登録者

Bowman, B.R.,Baker, M.L.,Rixon, F.J.,Chiu, W.,Quiocho, F.A. (登録日: 2003-01-15, 公開日: 2004-01-20, 最終更新日: 2024-02-14)

主引用文献

Bowman, B.R.,Baker, M.L.,Rixon, F.J.,Chiu, W.,Quiocho, F.A.
Structure of the herpesvirus major capsid protein
Embo J., 22:757-765, 2003

PubMed Abstract: Herpes simplex virus-1 (HSV-1) virions are large, complex enveloped particles containing a proteinaceous tegument layer connected to an icosahedral capsid. The major capsid protein, VP5 (149 kDa), makes up both types of capsomere, pentons and hexons. Limited trypsin digestion of VP5 identified a single stable 65 kDa fragment which represents a proposed protein folding nucleus. We report the 2.9 A crystal structure of this fragment and its modeling into an 8.5 A resolution electron cryomicroscopy map of the HSV-1 capsid. The structure, the first for any capsid protein from Herpesviridae, revealed a novel fold, placing herpesviruses outside any of the structurally linked viral groupings. Alterations in the geometrical arrangements of the VP5 subunits in the capsomeres exposes different residues, resulting in the differential association of the tegument and VP26 with the pentons and hexons, respectively. The rearrangements of VP5 subunits required to form both pentavalent and hexavalent capsomeres result in structures that exhibit very different electrostatic properties. These differences may mediate the binding and release of other structural proteins during capsid maturation.

PubMed: 12574112
DOI: 10.1093/emboj/cdg086

実験手法

X-RAY DIFFRACTION (2.9 Å)