1DOR

DIHYDROOROTATE DEHYDROGENASE A FROM LACTOCOCCUS LACTIS

1DOR の概要

• エントリーDOI: 10.2210/pdb1dor/pdb
• 分子名称: DIHYDROOROTATE DEHYDROGENASE A, FLAVIN MONONUCLEOTIDE (3 entities in total)
• 機能のキーワード: oxidoreductase, pyrimidine nucleotide biosynthesis
• 由来する生物種: Lactococcus lactis
• 細胞内の位置: Cytoplasm (By similarity): P54321
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 69397.02

構造登録者

Rowland, P.,Larsen, S. (登録日: 1997-01-14, 公開日: 1997-04-21, 最終更新日: 2024-02-07)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2 Å)