Literature DB >> 12198302

Adenovirus proteinase: crystallization and preliminary X-ray diffraction studies to atomic resolution.

Mary Lynn Baniecki1, William J McGrath, Zbigniew Dauter, Walter F Mangel.   

Abstract

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.

Entities:  

Mesh:

Substances:

Year:  2002        PMID: 12198302     DOI: 10.1107/S0907444902008429

Source DB:  PubMed          Journal:  Acta Crystallogr D Biol Crystallogr        ISSN: 0907-4449


  1 in total

1.  Regulation of a viral proteinase by a peptide and DNA in one-dimensional space: III. atomic resolution structure of the nascent form of the adenovirus proteinase.

Authors:  Mary Lynn Baniecki; William J McGrath; Walter F Mangel
Journal:  J Biol Chem       Date:  2012-10-07       Impact factor: 5.157

  1 in total

北京卡尤迪生物科技股份有限公司 © 2022-2023.