3MPG

Dihydroorotase from Bacillus anthracis

Summary for 3MPG

• Entry DOI: 10.2210/pdb3mpg/pdb
• Descriptor: Dihydroorotase, ZINC ION (3 entities in total)
• Functional Keywords: hydrolase
• Biological source: Bacillus anthracis (anthrax)
• Total number of polymer chains: 2
• Total formula weight: 93698.20

Authors

Santarsiero, B.D.,Mehboob, S.,Johnson, M.E. (deposition date: 2010-04-26, release date: 2010-11-10, Last modification date: 2024-02-21)

Primary citation

Mehboob, S.,Mulhearn, D.C.,Truong, K.,Johnson, M.E.,Santarsiero, B.D.
Structure of dihydroorotase from Bacillus anthracis at 2.6A resolution.
Acta Crystallogr.,Sect.F, 66:1432-1435, 2010

PubMed 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.

PubMed: 21045288
DOI: 10.1107/S1744309110037085

Experimental method

X-RAY DIFFRACTION (2.6 Å)