Structural highlights
Function
PYRC_METJA Catalyzes the reversible cyclization of carbamoyl aspartate to dihydroorotate.
Publication Abstract from PubMed
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 beta sandwich domain adjacent to the TIM barrel. Loop 5 is similar to bacterial type III and the C-terminal extension is long.
Crystal structure of Methanococcus jannaschii dihydroorotase.,Vitali J, Nix JC, Newman HE, Colaneri MJ Proteins. 2022 Aug 17. doi: 10.1002/prot.26412. PMID:35978488[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
