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Structure of dihydroorotase from Bacillus anthracis at 2.6 Å resolution

Structure of dihydroorotase from Bacillus anthracis at 2.6 Å resolution 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. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Acta Crystallographica Section F Wiley

Structure of dihydroorotase from Bacillus anthracis at 2.6 Å resolution

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References (16)

Publisher
Wiley
Copyright
International Union of Crystallography, 2010
ISSN
1744-3091
eISSN
1744-3091
DOI
10.1107/S1744309110037085
pmid
21045288
Publisher site
See Article on Publisher Site

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.

Journal

Acta Crystallographica Section FWiley

Published: Nov 1, 2010

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