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Structure of purine nucleoside phosphorylase (DeoD) from Bacillus anthracis.
- Source :
-
Acta crystallographica. Section F, Structural biology and crystallization communications [Acta Crystallogr Sect F Struct Biol Cryst Commun] 2005 May 01; Vol. 61 (Pt 5), pp. 459-62. Date of Electronic Publication: 2005 Apr 09. - Publication Year :
- 2005
-
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.
- Subjects :
- Amino Acid Sequence
Bacillus anthracis metabolism
Cloning, Organism
Crystallography, X-Ray
Models, Molecular
Molecular Sequence Data
Protein Conformation
Protein Structure, Secondary
Purine-Nucleoside Phosphorylase metabolism
Sequence Alignment
Spectrometry, Mass, Electrospray Ionization
Bacillus anthracis enzymology
Purine-Nucleoside Phosphorylase chemistry
Subjects
Details
- Language :
- English
- ISSN :
- 1744-3091
- Volume :
- 61
- Issue :
- Pt 5
- Database :
- MEDLINE
- Journal :
- Acta crystallographica. Section F, Structural biology and crystallization communications
- Publication Type :
- Academic Journal
- Accession number :
- 16511068
- Full Text :
- https://doi.org/10.1107/S174430910501095X