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 observe...

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Bibliographic Details
Published in:Acta crystallographica. Section D, Biological crystallography. Biological crystallography., 2002-09, Vol.58 (9), p.1462-1464
Main Authors: Baniecki, Mary Lynn, McGrath, William J., Dauter, Zbigniew, Mangel, Walter F.
Format: Article
Language:English
Subjects:
Adenoviridae - enzymology
Adenoviridae - genetics
adenovirus proteinase
Cloning, Molecular
Crystallography, X-Ray
Endopeptidases - chemistry
Protein Conformation
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Summary: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 Å and an isomorphous heavy‐atom derivative diffracted to 1.9 Å. 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.
ISSN:1399-0047
0907-4449
1399-0047
DOI:10.1107/S0907444902008429