Journal
EMBO JOURNAL
Volume 20, Issue 7, Pages 1485-1497Publisher
WILEY
DOI: 10.1093/emboj/20.7.1485
Keywords
capsid protein; crystal structure; icosahedral virus; quasi-equivalence; rotavirus
Categories
Ask authors/readers for more resources
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 Angstrom 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 Zn2+ 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.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available