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

• Published in: Acta crystallographica. Section D, Biological crystallography. Vol. 67; no. 10; pp. 870 - 874
• Main Authors: Tuntland, Micheal L., Johnson, Michael E., Fung, L. W.-M., Santarsiero, Bernard D.
• Format: Journal Article
• Language: English
• Published: 5 Abbey Square, Chester, Cheshire CH1 2HU, England International Union of Crystallography 01.10.2011
• 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
• ISSN: 1399-0047; 0907-4449; 1399-0047
• DOI: 10.1107/S0907444911029210

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.