Structure of purine nucleoside phosphorylase (DeoD) from Bacillus anthracis.
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.
Grenha
Rosa
R
Department of Chemistry, University of York, York YO10 5YW, England.
Levdikov
Vladimir M
VM
Fogg
Mark J
MJ
Blagova
Elena V
EV
Brannigan
James A
JA
Wilkinson
Anthony J
AJ
Wilson
Keith S
KS
D000595:Amino Acid Sequence; D001408:Bacillus anthracis / Q000201:enzymology* / Q000378:metabolism; D019976:Cloning, Organism; D018360:Crystallography, X-Ray; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011487:Protein Conformation; D017433:Protein Structure, Secondary; D011683:Purine-Nucleoside Phosphorylase / Q000737:chemistry* / Q000378:metabolism; D016415:Sequence Alignment; D021241:Spectrometry, Mass, Electrospray Ionization
D011683:Purine-Nucleoside Phosphorylase