ATP Binding and ATPase Activities Associated with Recombinant Rabbit Hemorrhagic Disease Virus 2C-Like Polypeptide
Open Access
- 15 November 2000
- journal article
- Published by American Society for Microbiology in Journal of Virology
- Vol. 74 (22) , 10846-10851
- https://doi.org/10.1128/jvi.74.22.10846-10851.2000
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-Δ2C 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.Keywords
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