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Structure of purine nucleoside phosphorylase (DeoD) from Bacillus anthracis

By R Grenha, V M Levdikov, M J Fogg, E V Blagova, J A Brannigan, A.J. Wilkinson and K S Wilson

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 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

Year: 2005
OAI identifier: oai:eprints.whiterose.ac.uk:434

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