1QHD

CRYSTAL STRUCTURE OF VP6, THE MAJOR CAPSID PROTEIN OF GROUP A ROTAVIRUS

1QHD の概要

• エントリーDOI: 10.2210/pdb1qhd/pdb
• 分子名称: VIRAL CAPSID VP6, ZINC ION, CHLORIDE ION, ... (5 entities in total)
• 機能のキーワード: viral capsid protein, viral protein
• 由来する生物種: Bovine rotavirus
• 細胞内の位置: Virion: P04509
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 45206.93

構造登録者

Mathieu, M.,Petitpas, I.,Rey, F.A. (登録日: 1999-04-29, 公開日: 2001-04-13, 最終更新日: 2024-10-30)

主引用文献

Mathieu, M.,Petitpas, I.,Navaza, J.,Lepault, J.,Kohli, E.,Pothier, P.,Prasad, B.V.,Cohen, J.,Rey, F.A.
Atomic structure of the major capsid protein of rotavirus: implications for the architecture of the virion.
EMBO J., 20:1485-1497, 2001

PubMed Abstract: The structural protein VP6 of rotavirus, an important pathogen responsible for severe gastroenteritis in children, forms the middle layer in the triple-layered viral capsid. Here we present the crystal structure of VP6 determined to 2 A resolution and describe its interactions with other capsid proteins by fitting the atomic model into electron cryomicroscopic reconstructions of viral particles. VP6, which forms a tight trimer, has two distinct domains: a distal beta-barrel domain and a proximal alpha-helical domain, which interact with the outer and inner layer of the virion, respectively. The overall fold is similar to that of protein VP7 from bluetongue virus, with the subunits wrapping about a central 3-fold axis. A distinguishing feature of the VP6 trimer is a central Zn(2+) ion located on the 3-fold molecular axis. The crude atomic model of the middle layer derived from the fit shows that quasi-equivalence is only partially obeyed by VP6 in the T = 13 middle layer and suggests a model for the assembly of the 260 VP6 trimers onto the T = 1 viral inner layer.

PubMed: 11285213
DOI: 10.1093/emboj/20.7.1485

実験手法

X-RAY DIFFRACTION (1.95 Å)