Structure of purine nucleoside phosphorylase (DeoD) from Bacillus anthracis

Grenha, R, Levdikov, V M, Fogg, M J, Blagova, E V, Brannigan, J A, Wilkinson, A.J. and Wilson, K S (2005) Structure of purine nucleoside phosphorylase (DeoD) from Bacillus anthracis. Acta Crystallographica Section F: Structural Biology and Crystallization Communications. pp. 459-462. ISSN 1744-3091

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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.

Item Type:	Article
Copyright, Publisher and Additional Information:	Copyright © 2005 International Union of Crystallography - http://www.iucr.org/cgi-bin/paper?gx5050
Keywords:	CRYSTAL-STRUCTURE, ESCHERICHIA-COLI, SEQUENCE, DISTINCT, MODEL
Academic Units:	The University of York > Chemistry (York)
Depositing User:	Repository Officer
Date Deposited:	11 May 2005
Last Modified:	19 Feb 2013 11:49
Published Version:	http://dx.doi.org/10.1107/S174430910501095X
Status:	Published
Refereed:	Yes
Related URLs:	http://www.iucr.org/cgi-bin/paper?gx5050
URI:	http://eprints.whiterose.ac.uk/id/eprint/434

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