Structure of N5-carboxyaminoimidazole ribonucleotide synthase (PurK) from Bacillus anthracis

The apo structure of N5‐carboxyaminoimidazole ribonucleotide synthase (PurK) from Bacillus anthracis (baPurK) with Mg2+ in the active site is reported at 1.96 Å resolution. PurK is an enzyme in the purine‐biosynthetic pathway, unique to prokaryotes, that converts 5‐aminoimidazole ribonucleotide to N...

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Bibliographic Details
Published in:Acta crystallographica. Section D, Biological crystallography. Biological crystallography., 2011-10, Vol.67 (10), p.870-874
Main Authors: Tuntland, Micheal L., Johnson, Michael E., Fung, L. W.-M., Santarsiero, Bernard D.
Format: Article
Language:English
Subjects:
Bacillus anthracis
Bacillus anthracis - enzymology
Bacterial Proteins - chemistry
Binding Sites
Catalytic Domain
Crystallography, X-Ray
Imidazoles - metabolism
Ligases - chemistry
Ligases - metabolism
Magnesium - metabolism
N5-carboxyaminoimidazole ribonucleotide synthase
Protein Conformation
purine biosynthesis
PurK
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Summary:The apo structure of N5‐carboxyaminoimidazole ribonucleotide synthase (PurK) from Bacillus anthracis (baPurK) with Mg2+ in the active site is reported at 1.96 Å resolution. PurK is an enzyme in the purine‐biosynthetic pathway, unique to prokaryotes, that converts 5‐aminoimidazole ribonucleotide to N5‐carboxyaminoimidazole ribonucleotide and has been suggested as a potential antimicrobial drug target. Two interesting features of baPurK are a flexible B‐loop (residues 149/150–157) that is in close contact with the active site and the binding of Mg2+ to the active site without additional ligands.
ISSN:1399-0047
0907-4449
1399-0047
DOI:10.1107/S0907444911029210