ATP binding and ATPase activities associated with recombinant rabbit hemorrhagic disease virus 2C-like polypeptide.

ABSTRACT: The carboxy-terminal region of the rabbit hemorrhagic disease virus p37 polyprotein cleavage product has been expressed in Escherichia coli as a glutathione S-transferase (GST) fusion protein. The recombinant GST-Delta2C protein showed in vitro ATP-binding and ATPase activities. Site-directed mutagenesis studies of the conserved residues G(522) and T(529) in motif A, D(566) and E(567) in motif B, and K(600) in motif C were also performed. These results provide the first experimental characterization of a 2C-like ATPase activity in a member of the Caliciviridae.

SUBMITTER: Marin MS 

PROVIDER: S-EPMC110965 | biostudies-literature | 2000 Nov

REPOSITORIES: biostudies-literature