7UOF

Dihydroorotase from M. jannaschii

7UOF の概要

• エントリーDOI: 10.2210/pdb7uof/pdb
• 分子名称: Dihydroorotase, ZINC ION (3 entities in total)
• 機能のキーワード: hydrolase, de novo pyrimidine biosynthesis, amidohydrolase superfamily, metalloenzyme, zinc binding, histidinate anion
• 由来する生物種: Methanocaldococcus jannaschii
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 48945.52

構造登録者

Vitali, J.,Nix, J.C.,Newman, H.E.,Colaneri, M.J. (登録日: 2022-04-12, 公開日: 2022-08-31, 最終更新日: 2023-11-15)

主引用文献

Vitali, J.,Nix, J.C.,Newman, H.E.,Colaneri, M.J.
Crystal structure of Methanococcus jannaschii dihydroorotase.
Proteins, 91:91-98, 2023

PubMed Abstract: In this paper, we report the structural analysis of dihydroorotase (DHOase) from the hyperthermophilic and barophilic archaeon Methanococcus jannaschii. DHOase catalyzes the reversible cyclization of N-carbamoyl-l-aspartate to l-dihydroorotate in the third step of de novo pyrimidine biosynthesis. DHOases form a very diverse family of enzymes and have been classified into types and subtypes with structural similarities and differences among them. This is the first archaeal DHOase studied by x-ray diffraction. Its structure and comparison with known representatives of the other subtypes help define the structural features of the archaeal subtype. The M. jannaschii DHOase is found here to have traits from all subtypes. Contrary to expectations, it has a carboxylated lysine bridging the two Zn ions in the active site, and a long catalytic loop. It is a monomeric protein with a large β sandwich domain adjacent to the TIM barrel. Loop 5 is similar to bacterial type III and the C-terminal extension is long.

PubMed: 35978488
DOI: 10.1002/prot.26412

実験手法

X-RAY DIFFRACTION (1.9 Å)