Crystal structure of Methanococcus jannaschii dihydroorotase.
Methanococcus jannaschii
crystal structure
dihydroorotase
pyrimidine biosynthesis
Journal
Proteins
ISSN: 1097-0134
Titre abrégé: Proteins
Pays: United States
ID NLM: 8700181
Informations de publication
Date de publication:
01 2023
01 2023
Historique:
revised:
02
08
2022
received:
29
04
2022
accepted:
11
08
2022
pubmed:
19
8
2022
medline:
16
12
2022
entrez:
18
8
2022
Statut:
ppublish
Résumé
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.
Identifiants
pubmed: 35978488
doi: 10.1002/prot.26412
pmc: PMC9771888
mid: NIHMS1830629
doi:
Substances chimiques
Dihydroorotase
EC 3.5.2.3
Aspartic Acid
30KYC7MIAI
Types de publication
Journal Article
Research Support, N.I.H., Extramural
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
91-98Subventions
Organisme : NIGMS NIH HHS
ID : P30 GM124169
Pays : United States
Organisme : NIGMS NIH HHS
ID : R15 GM071512
Pays : United States
Organisme : NCI NIH HHS
ID : T32 CA009615
Pays : United States
Informations de copyright
© 2022 The Authors. Proteins: Structure, Function, and Bioinformatics published by Wiley Periodicals LLC.
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