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Structures of feline immunodeficiency virus dutp pyrophosphatase and its nucleotide complexes in three crystal forms

Academic Article
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Overview

authors

  • Prasad, G. S.
  • Stura, E. A.
  • Elder, John
  • Stout, C. David

publication date

  • September 2000

journal

  • Acta Crystallographica Section D-Biological Crystallography  Journal

abstract

  • dUTP pyrophosphatase (dUTPase) cleaves the alpha-beta phosphodiester of dUTP to form pyrophosphate and dUMP, preventing incorporation of uracil into DNA and providing the substrate for thymine synthesis. Seven crystal structures of feline immunodeficiency virus (FIV) dUTPase in three crystal forms have been determined, including complexes with substrate (dUTP), product (dUMP) or inhibitor (dUDP) bound. The native enzyme has been refined at 1.40 A resolution in a hexagonal crystal form and at 2.3 A resolution in an orthorhombic crystal form. In the dUDP complex in a cubic crystal form refined at 2.5 A resolution, the C-terminal conserved P-loop motif is fully ordered. The analysis defines the roles of five sequence motifs in interaction with uracil, deoxyribose and the alpha-, beta- and gamma-phosphates. The enzyme utilizes adaptive recognition to bind the alpha- and beta-phosphates. In particular, the alpha-beta phosphodiester adopts an unfavorable eclipsed conformation in the presence of the P-loop. This conformation may be relevant to the mechanism of alpha-beta phosphodiester bond cleavage.

subject areas

  • Animals
  • Cats
  • Crystallization
  • Crystallography, X-Ray
  • Deoxyuracil Nucleotides
  • Immunodeficiency Virus, Feline
  • Models, Molecular
  • Protein Conformation
  • Protein Structure, Secondary
  • Pyrophosphatases
  • Viral Proteins
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Identity

International Standard Serial Number (ISSN)

  • 0907-4449

Digital Object Identifier (DOI)

  • 10.1107/s0907444900009197

PubMed ID

  • 10957629
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Additional Document Info

start page

  • 1100

end page

  • 1109

volume

  • 56

issue

  • Pt 9

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