Adenovirus proteinase: crystallization and preliminary X-ray diffraction studies to atomic resolution.
Adenovirus proteinase (AVP) is required for the synthesis of infectious virus and is a target for antiviral therapy. The enzyme requires two viral cofactors for activation: pVIc, an 11-amino acid peptide, and the viral DNA. The structure of the enzyme in the absence of cofactors has not been observed. Single crystals of AVP were obtained via microseeding using the hanging-drop vapour-diffusion method with sodium acetate and sodium citrate as precipitants. At the National Synchrotron Light Source at Brookhaven National Laboratory, the native crystal diffracted to a resolution of 0.98 A and an isomorphous heavy-atom derivative diffracted to 1.9 A. Comparison of the structure of AVP with that of the AVP-pVIc complex should reveal the structural basis of activation of the enzyme by pVIc.
Baniecki
Mary Lynn
ML
Department of Pharmacological Sciences, State University of New York at Stony Brook, 11794, USA.
McGrath
William J
WJ
Dauter
Zbigniew
Z
Mangel
Walter F
WF
D000256:Adenoviridae / Q000201:enzymology* / Q000235:genetics; D003001:Cloning, Molecular; D018360:Crystallography, X-Ray; D010450:Endopeptidases / Q000737:chemistry*; D011487:Protein Conformation
D010450:Endopeptidases