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Atomic structure of the major capsid protein of rotavirus: implications for the architecture of the virion
Author(s) -
Mathieu Magali,
Petitpas Isabelle,
Navaza Jorge,
Lepault Jean,
Kohli Evelyne,
Pothier Pierre,
Prasad B.V.Venkataram,
Cohen Jean,
Rey Félix A.
Publication year - 2001
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1093/emboj/20.7.1485
Subject(s) - capsid , trimer , biology , rotavirus , virology , viral protein , crystallography , biophysics , virus , physics , chemistry , dimer , nuclear magnetic resonance
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 Å 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 β‐barrel domain and a proximal α‐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.