Crystal Structure of purine nucleoside phosphorylase DeoD from Bacillus anthracisCrystal Structure of purine nucleoside phosphorylase DeoD from Bacillus anthracis

Structural highlights

1xe3 is a 6 chain structure with sequence from Bacillus anthracis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.24Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

DEOD_BACAN

Evolutionary Conservation

 

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

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.

Structure of purine nucleoside phosphorylase (DeoD) from Bacillus anthracis.,Grenha R, Levdikov VM, Fogg MJ, Blagova EV, Brannigan JA, Wilkinson AJ, Wilson KS Acta Crystallogr Sect F Struct Biol Cryst Commun. 2005 May 1;61(Pt, 5):459-62. Epub 2005 Apr 9. PMID:16511068[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. Grenha R, Levdikov VM, Fogg MJ, Blagova EV, Brannigan JA, Wilkinson AJ, Wilson KS. Structure of purine nucleoside phosphorylase (DeoD) from Bacillus anthracis. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2005 May 1;61(Pt, 5):459-62. Epub 2005 Apr 9. PMID:16511068 doi:10.1107/S174430910501095X

1xe3, resolution 2.24Å

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