Temporal and spatial control of the adenovirus proteinase by both a peptide and the viral DNA.
The adenovirus proteinase (AVP) uses both an 11-amino acid peptide (pVIc) and the viral DNA as cofactors to increase its catalytic rate constant 6000-fold. The crystal structure of an AVP-pVIc complex at 2.6-A resolution reveals a new protein fold of an enzyme that is the first member of a new class of cysteine proteinases, which arose via convergent evolution.
Mangel
W F
WF
Biology Department, Brookhaven National Laboratory, Upton, NY 11973-5000, USA. mangel@bnl.gov
Toledo
D L
DL
Ding
J
J
Sweet
R M
RM
McGrath
W J
WJ
D000256:Adenoviridae / Q000201:enzymology*; D003546:Cysteine Endopeptidases / Q000378:metabolism*; D004279:DNA, Viral / Q000502:physiology*; D008958:Models, Molecular; D017433:Protein Structure, Secondary; D013997:Time Factors
D004279:DNA, Viral; D003546:Cysteine Endopeptidases