3Q2O

Crystal Structure of purK: N5-carboxyaminoimidazole ribonucleotide synthetase

Summary for 3Q2O

• Entry DOI: 10.2210/pdb3q2o/pdb
• Descriptor: Phosphoribosylaminoimidazole carboxylase, ATPase subunit, MAGNESIUM ION (3 entities in total)
• Functional Keywords: carboxylase, carboxylates, atp binding, lyase
• Biological source: Bacillus anthracis
• Total number of polymer chains: 2
• Total formula weight: 86467.32

Authors

Fung, L.W.,Tuntland, M.L.,Santarsiero, B.D.,Johnson, M.E. (deposition date: 2010-12-20, release date: 2011-10-26, Last modification date: 2023-09-13)

Primary citation

Tuntland, M.L.,Johnson, M.E.,Fung, L.W.,Santarsiero, B.D.
Structure of N(5)-carboxyaminoimidazole ribonucleotide synthase (PurK) from Bacillus anthracis.
Acta Crystallogr.,Sect.D, 67:870-874, 2011

PubMed 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.

PubMed: 21931218
DOI: 10.1107/S0907444911029210

Experimental method

X-RAY DIFFRACTION (1.96 Å)