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.
Center for Pharmaceutical Biotechnology and the Department of Medicinal Chemistry and Pharmacognosy, University of Illinois at Chicago, MC-870, 900 South Ashland Avenue, Chicago, IL 60607-7173, USA.
Shahila
S
Mehboob
Debbie C
DC
Mulhearn
Kent
K
Truong
Michael E
ME
Johnson
Bernard D
BD
Santarsiero
D000595:Amino Acid Sequence; D001408:Bacillus anthracis / Q000201:enzymology*; D018360:Crystallography, X-Ray; D004080:Dihydroorotase / Q000737:chemistry*; D008958:Models, Molecular; D008969:Molecular Sequence Data; D020836:Protein Structure, Quaternary; D017434:Protein Structure, Tertiary; D016415:Sequence Alignment; D040681:Structural Homology, Protein
D004080:Dihydroorotase