Ontology highlight
ABSTRACT:
SUBMITTER: Tuntland ML
PROVIDER: S-EPMC3270386 | biostudies-literature | 2011 Oct
REPOSITORIES: biostudies-literature
Tuntland Micheal L ML Johnson Michael E ME Fung L W-M LW Santarsiero Bernard D BD
Acta crystallographica. Section D, Biological crystallography 20110908 Pt 10
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 ...[more]