Abstract:The apo structure of N 5‐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 5‐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.
Document Type: Research Article
Publication date: October 1, 2011