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

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Title: Structure of N5-carboxyaminoimidazole ribonucleotide synthase (PurK) from Bacillus anthracis
Author(s): Tuntland, M. L.; Johnson, M. E.; Fung, L.; Santarsiero, B. D.
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 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.
Issue Date: 2011-10
Publisher: International Union of Crystallography
Citation Info: Tuntland, M. L., Johnson, M. E., Fung, L., & Santarsiero, B. D. 2011. Structure of N(5)-carboxyaminoimidazole ribonucleotide synthase (PurK) from Bacillus anthracis. Acta Crystallographica Section D-Biological Crystallography, 67: 870-874. DOI: 10.1107/S0907444911029210
Type: Article
Description: This is a copy of an article published in the Acta Crystallographica Section D-Biological Crystallography © 2011 International Union of Crystallography. DOI: 10.1107/S0907444911029210
URI: http://hdl.handle.net/10027/8169
ISSN: 0907-4449
Date Available in INDIGO: 2012-03-06
 

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