Open AccessStructure of dihydroorotase from Bacillus anthracis at 2.6 Å resolution
Author(s) -
Mehboob Shahila,
Mulhearn Debbie C.,
Truong Kent,
Johnson Michael E.,
Santarsiero Bernard D.
Publication year - 2010
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309110037085
Subject(s) - bacillus anthracis , aspartate carbamoyltransferase , dimer , biochemistry , biology , chemistry , stereochemistry , enzyme , bacteria , allosteric regulation , genetics , organic chemistry
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.