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Structure of dihydroorotase from Bacillus anthracis at 2.6 A resolution

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Title: Structure of dihydroorotase from Bacillus anthracis at 2.6 A resolution
Author(s): Mehboob, Shahila; Mulhearn, Debbie C.; Truong, Kent; Johnson, Michael E.; Santarsiero, Bernard D.
Subject(s): structure comparison
Abstract: Dihydroorotase (EC 3.5.2.3) catalyzes the reversible cyclization of N-carbamoyl-l-aspartate to l-dihydroorotate in the third step of the pyrimidine-biosynthesis pathway in Bacillus anthracis. A comparison is made between the structures of dihydroorotase from four different organisms, including B. anthracis dihydroorotase, and reveals substantial variations in the active site, dimer interface and overall tertiary structure. These differences demonstrate the utility of exploring multiple structures of a molecular target as expressed from different organisms and how these differences can be exploited for structure-based drug discovery.
Issue Date: 2010-11
Publisher: International Union of Crystallography
Citation Info: Mehboob, S., Mulhearn, D. C., Truong, K., Johnson, M. E., & Santarsiero, B. D. 2010. Structure of dihydroorotase from Bacillus anthracis at 2.6 A resolution. Acta Crystallographica Section F-Structural Biology and Crystallization Communications, 66: 1432-1435. DOI: 10.1107/S1744309110037085
Type: Article
Description: The original publication is available through the International Union of Crystallography at DOI: 10.1107/S1744309110037085.
URI: http://hdl.handle.net/10027/7724
ISSN: 1744-3091
Sponsor: We acknowledge the use of the Advanced Photon Source, which is supported by the US Department of Energy, Basic Energy Sciences, Office of Science under contract No. DE-AC02-06CH11357. NE-CAT Sector 24 is supported by the National Institutes of Health, National Center for Research Resources under grant No. RR-15301.
Date Available in INDIGO: 2011-05-27
 

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