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

Authors
Marin, MS Casais, R Alonso, JMM Parra, F
Citation
Ms. Marin et al., ATP binding and ATPase activities associated with recombinant rabbit hemorrhagic disease virus 2C-like polypeptide, J VIROLOGY, 74(22), 2000, pp. 10846-10851
Citations number
31
Categorie Soggetti
Microbiology
Journal title
JOURNAL OF VIROLOGY
ISSN journal
0022538X → ACNP
Volume
74
Issue
22
Year of publication
2000
Pages
10846 - 10851
Database
ISI
SICI code
0022-538X(200011)74:22<10846:ABAAAA>2.0.ZU;2-8
Abstract
The carboxy-terminal region of the rabbit hemorrhagic disease virus p37 pol yprotein cleavage product has been expressed in Escherichia coli as a gluta thione S-transferase (GST) fusion protein. The recombinant GST-Delta 2C pro tein showed in vitro ATP-binding and ATPase activities. Site directed mutag enesis 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 resu lts provide the first experimental characterization of a 2C-like ATPase act ivity in a member of the Caliciviridae.