Grenha, R, Levdikov, V M, Fogg, M J et al. (4 more authors) (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
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.
Metadata
Authors/Creators: |
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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 |
Dates: |
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Institution: | The University of York |
Academic Units: | The University of York > Faculty of Sciences (York) > Chemistry (York) |
Depositing User: | Repository Officer |
Date Deposited: | 11 May 2005 |
Last Modified: | 04 Feb 2024 00:26 |
Published Version: | https://doi.org/10.1107/S174430910501095X |
Status: | Published |
Refereed: | Yes |
Identification Number: | https://doi.org/10.1107/S174430910501095X |
Related URLs: |