Literature DB >> 21931218

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

Micheal L Tuntland1, Michael E Johnson, L W-M Fung, Bernard D Santarsiero.   

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.

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Year:  2011        PMID： 21931218      PMCID： PMC3270386          DOI： 10.1107/S0907444911029210

Source DB:  PubMed          Journal:  Acta Crystallogr D Biol Crystallogr        ISSN： 0907-4449


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