1F76

ESCHERICHIA COLI DIHYDROOROTATE DEHYDROGENASE

1F76 の概要

• エントリーDOI: 10.2210/pdb1f76/pdb
• 分子名称: Dihydroorotate dehydrogenase (quinone), FLAVIN MONONUCLEOTIDE, OROTIC ACID, ... (5 entities in total)
• 機能のキーワード: monomer, alpha-beta-barrel, fmn binding domain, orotate complex, oxidoreductase
• 由来する生物種: Escherichia coli
• 細胞内の位置: Cell membrane; Peripheral membrane protein: P0A7E1
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 151248.71

構造登録者

Norager, S.,Jensen, K.F.,Bjornberg, O.,Larsen, S. (登録日: 2000-06-26, 公開日: 2002-10-16, 最終更新日: 2024-12-25)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2.5 Å)