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

Authors :
Grenha R
Levdikov VM
Fogg MJ
Blagova EV
Brannigan JA
Wilkinson AJ
Wilson KS
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.

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