1DOR

DIHYDROOROTATE DEHYDROGENASE A FROM LACTOCOCCUS LACTIS

Summary for 1DOR

• Entry DOI: 10.2210/pdb1dor/pdb
• Descriptor: DIHYDROOROTATE DEHYDROGENASE A, FLAVIN MONONUCLEOTIDE (3 entities in total)
• Functional Keywords: oxidoreductase, pyrimidine nucleotide biosynthesis
• Biological source: Lactococcus lactis
• Cellular location: Cytoplasm (By similarity): P54321
• Total number of polymer chains: 2
• Total formula weight: 69397.02

Authors

Rowland, P.,Larsen, S. (deposition date: 1997-01-14, release date: 1997-04-21, Last modification date: 2024-02-07)

Primary citation

Rowland, P.,Nielsen, F.S.,Jensen, K.F.,Larsen, S.
The crystal structure of the flavin containing enzyme dihydroorotate dehydrogenase A from Lactococcus lactis.
Structure, 5:239-252, 1997

PubMed Abstract: . Dihydroorotate dehydrogenase (DHOD) is a flavin mononucleotide containing enzyme, which catalyzes the oxidation of (S)-dihydroorotate to orotate, the fourth step in the de novo biosynthesis of pyrimidine nucleotides. Lactococcus lactis contains two genes encoding different functional DHODs whose sequences are only 30% identical. One of these enzymes, DHODA, is a highly efficient dimer, while the other, DHODB, shows optimal activity only in the presence of an iron-sulphur cluster containing protein with which it forms a complex tetramer. Sequence alignments have identified three different families among the DHODs: the two L. lactis enzymes belong to two of the families, whereas the enzyme from E. coli is a representative of the third. As no three-dimensional structures of DHODs are currently available, we set out to determine the crystal structure of DHODA from L. lactis. The differences between the two L. lactis enzymes make them particularly interesting for studying flavoprotein redox reactions and for identifying the differences between the enzyme families.

PubMed: 9032071
DOI: 10.1016/S0969-2126(97)00182-2

Experimental method

X-RAY DIFFRACTION (2 Å)