Structure of purine nucleoside phosphorylase (DeoD) from Bacillus anthracis

Research output: Contribution to journalArticlepeer-review

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 Å resolution and refined to an R factor of 18.4%. This is the first report of a DeoD structure from a Gram-positive bacterium.
Original languageEnglish
Pages (from-to)459-462
Number of pages4
JournalActa Crystallographica Section F: Structural Biology and Crystallization Communications
Volume61
Issue number5
DOIs
Publication statusPublished - May 2005

Bibliographical note

Copyright © 2005 International Union of Crystallography - http://www.iucr.org/cgi-bin/paper?gx5050

Keywords

  • CRYSTAL-STRUCTURE
  • ESCHERICHIA-COLI
  • SEQUENCE
  • DISTINCT
  • MODEL

Cite this