Structure of purine nucleoside phosphorylase (DeoD) from Bacillus anthracis

Journal Article · Sun May 01 00:00:00 EDT 2005 · Acta Crystallographica. Section F

DOI:https://doi.org/10.1107/S174430910501095X· OSTI ID:22356010

Grenha, Rosa; Levdikov, Vladimir M.; Fogg, Mark J.; Blagova, Elena V.; Wilkinson, Anthony J.; Wilson, Keith S. ^[1]

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1. Structural Biology Laboratory, Department of Chemistry, University of York, York YO10 5YW (United Kingdom)

The crystal structure of purine nucleoside phosphorylase (DeoD) from B. anthracis was solved by X-ray crystallography using molecular replacement and refined at a resolution of 2.24 Å. 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.

• OSTI ID: 22356010
• Journal Information: Acta Crystallographica. Section F, Vol. 61, Issue Pt 5; Other Information: PMCID: PMC1952315; PMID: 16511068; PUBLISHER-ID: gx5050; OAI: oai:pubmedcentral.nih.gov:1952315; Copyright (c) International Union of Crystallography 2005; Country of input: International Atomic Energy Agency (IAEA); ISSN 1744-3091
• Country of Publication: United Kingdom
• Language: English

Related Subjects

75 CONDENSED MATTER PHYSICS
SUPERCONDUCTIVITY AND SUPERFLUIDITY
CRYSTAL STRUCTURE
CRYSTALLOGRAPHY
POTENTIALS
PROTEIN STRUCTURE
R FACTORS
RESOLUTION