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Structure of purine nucleoside phosphorylase (DeoD) from Bacillus anthracis.


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.

SUBMITTER: Grenha R 

PROVIDER: S-EPMC1952315 | biostudies-literature | 2005 May

REPOSITORIES: biostudies-literature

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Structure of purine nucleoside phosphorylase (DeoD) from Bacillus anthracis.

Grenha Rosa R   Levdikov Vladimir M VM   Fogg Mark J MJ   Blagova Elena V EV   Brannigan James A JA   Wilkinson Anthony J AJ   Wilson Keith S KS  

Acta crystallographica. Section F, Structural biology and crystallization communications 20050409 Pt 5


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  ...[more]

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