ATP binding and ATPase activities associated with recombinant rabbit hemorrhagic disease virus 2C-like polypeptide |
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| Authors: | Marín M S Casais R Alonso J M Parra F |
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| Affiliation: | Departamento de Bioquímica y Biología Molecular, Instituto Universitario de Biotecnología de Asturias (CSIC), Universidad de Oviedo, 33006 Oviedo, Spain. |
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| 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. |
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