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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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

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.[1]

References

  1. ATP binding and ATPase activities associated with recombinant rabbit hemorrhagic disease virus 2C-like polypeptide. Marín, M.S., Casais, R., Alonso, J.M., Parra, F. J. Virol. (2000) [Pubmed]
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