Open AccessStructure of purine nucleoside phosphorylase (DeoD) from Bacillus anthracis
Author(s) -
Grenha Rosa,
Fogg Mark J.,
Blagova Elena V.,
Levdikov Vladimir M.,
Wilson Keith S.,
Wilkinson Anthony J.,
Brannigan James A.
Publication year - 2005
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s174430910501095x
Subject(s) - bacillus anthracis , purine nucleoside phosphorylase , nucleotide salvage , purine , enzyme , biochemistry , nucleotide , nucleoside , chemistry , purine metabolism , stereochemistry , biology , bacteria , gene , genetics
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.