ATP Binding and ATPase Activities Associated with Recombinant Rabbit Hemorrhagic Disease Virus 2C-Like Polypeptide
2000 ◽
Vol 74
(22)
◽
pp. 10846-10851
◽
Keyword(s):
ABSTRACT The carboxy-terminal region of the rabbit hemorrhagic disease virus p37 polyprotein cleavage product has been expressed inEscherichia 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 G522 and T529 in motif A, D566 and E567 in motif B, and K600 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.
1996 ◽
Vol 70
(12)
◽
pp. 8614-8623
◽
2016 ◽
Vol 65
◽
pp. 280-288
◽
1998 ◽
Vol 71
(1)
◽
pp. 27-33
◽
1998 ◽
Vol 72
(4)
◽
pp. 2999-3004
◽
2009 ◽
Vol 71
(11)
◽
pp. 1519-1523
◽
1994 ◽
Vol 68
(10)
◽
pp. 6487-6495
◽
1996 ◽
Vol 70
(11)
◽
pp. 7974-7983
◽
2016 ◽
Vol 237
◽
pp. 86-91
◽
2007 ◽
Vol 152
(6)
◽
pp. 1215-1221
◽