Structure of purine nucleoside phosphorylase (DeoD) from Bacillus anthracis

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2005 May 1;61(Pt 5):459-62. doi: 10.1107/S174430910501095X. Epub 2005 Apr 9.

Abstract

Protein structures from the causative agent of anthrax (Bacillus anthracis) are being determined as part of a structural genomics programme. Amongst initial candidates for crystallographic analysis are enzymes involved in nucleotide biosynthesis, since these are recognized as potential targets in antibacterial therapy. Purine nucleoside phosphorylase is a key enzyme in the purine-salvage pathway. The crystal structure of purine nucleoside phosphorylase (DeoD) from B. anthracis has been solved by molecular replacement at 2.24 A resolution and refined to an R factor of 18.4%. This is the first report of a DeoD structure from a Gram-positive bacterium.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Bacillus anthracis / enzymology*
  • Bacillus anthracis / metabolism
  • Cloning, Organism
  • Crystallography, X-Ray
  • Models, Molecular
  • Molecular Sequence Data
  • Protein Conformation
  • Protein Structure, Secondary
  • Purine-Nucleoside Phosphorylase / chemistry*
  • Purine-Nucleoside Phosphorylase / metabolism
  • Sequence Alignment
  • Spectrometry, Mass, Electrospray Ionization

Substances

  • Purine-Nucleoside Phosphorylase

Associated data

  • PDB/1XE3
  • PDB/R1XE3SF