1qhd

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spinqualitylabelsall models 1qhd, resolution 1.95Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

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

Overview

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.

About this Structure

1QHD is a Single protein structure of sequence from Bovine rotavirus with ZN, CL, CA and ACE as ligands. Full crystallographic information is available from OCA.

Reference

Atomic structure of the major capsid protein of rotavirus: implications for the architecture of the virion., Mathieu M, Petitpas I, Navaza J, Lepault J, Kohli E, Pothier P, Prasad BV, Cohen J, Rey FA, EMBO J. 2001 Apr 2;20(7):1485-97. PMID:11285213

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