1QHD

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

Summary for 1QHD

• Entry DOI: 10.2210/pdb1qhd/pdb
• Descriptor: VIRAL CAPSID VP6, ZINC ION, CHLORIDE ION, ... (5 entities in total)
• Functional Keywords: viral capsid protein, viral protein
• Biological source: Bovine rotavirus
• Cellular location: Virion: P04509
• Total number of polymer chains: 1
• Total formula weight: 45206.93

Authors

Mathieu, M.,Petitpas, I.,Rey, F.A. (deposition date: 1999-04-29, release date: 2001-04-13, Last modification date: 2024-10-30)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (1.95 Å)