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.
Original language | English |
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Pages (from-to) | 459-462 |
Number of pages | 4 |
Journal | Acta Crystallographica Section F: Structural Biology and Crystallization Communications |
Volume | 61 |
Issue number | 5 |
DOIs | |
Publication status | Published - May 2005 |
Bibliographical note
Copyright © 2005 International Union of Crystallography - http://www.iucr.org/cgi-bin/paper?gx5050Keywords
- CRYSTAL-STRUCTURE
- ESCHERICHIA-COLI
- SEQUENCE
- DISTINCT
- MODEL