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

ABSTRACT: 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.

SUBMITTER: Tuntland ML 

PROVIDER: S-EPMC3270386 | biostudies-literature | 2011 Oct

REPOSITORIES: biostudies-literature