3q2o

Publication Abstract from PubMed

The apo structure of N5-carboxyaminoimidazole ribonucleotide synthase (PurK) from Bacillus anthracis (baPurK) with Mg2+ in the active site is reported at 1.96 A 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.

Structure of N5-carboxyaminoimidazole ribonucleotide synthase (PurK) from Bacillus anthracis.,Tuntland ML, Johnson ME, Fung LW, Santarsiero BD Acta Crystallogr D Biol Crystallogr. 2011 Oct;67(Pt 10):870-4. Epub 2011, Sep 8. PMID:21931218^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.