1F76

ESCHERICHIA COLI DIHYDROOROTATE DEHYDROGENASE

Summary for 1F76

• Entry DOI: 10.2210/pdb1f76/pdb
• Descriptor: Dihydroorotate dehydrogenase (quinone), FLAVIN MONONUCLEOTIDE, OROTIC ACID, ... (5 entities in total)
• Functional Keywords: monomer, alpha-beta-barrel, fmn binding domain, orotate complex, oxidoreductase
• Biological source: Escherichia coli
• Cellular location: Cell membrane; Peripheral membrane protein: P0A7E1
• Total number of polymer chains: 4
• Total formula weight: 151248.71

Authors

Norager, S.,Jensen, K.F.,Bjornberg, O.,Larsen, S. (deposition date: 2000-06-26, release date: 2002-10-16, Last modification date: 2024-12-25)

Primary citation

Norager, S.,Jensen, K.F.,Bjornberg, O.,Larsen, S.
E. coli Dihydroorotate Dehydrogenase Reveals Structural and Functional Distinction between different classes of dihydroorotate dehydrogenases
Structure, 10:1211-1223, 2002

PubMed Abstract: The flavoenzymes dihydroorotate dehydrogenases (DHODs) catalyze the fourth and only redox step in the de novo biosynthesis of UMP. Enzymes belonging to class 2, according to their amino acid sequence, are characterized by having a serine residue as the catalytic base and a longer N terminus. The structure of class 2 E. coli DHOD, determined by MAD phasing, showed that the N-terminal extension forms a separate domain. The catalytic serine residue has an environment differing from the equivalent cysteine in class 1 DHODs. Significant differences between the two classes of DHODs were identified by comparison of the E. coli DHOD with the other known DHOD structures, and differences with the class 2 human DHOD explain the variation in their inhibitors.

PubMed: 12220493
DOI: 10.1016/S0969-2126(02)00831-6

Experimental method

X-RAY DIFFRACTION (2.5 Å)