Structure of dihydroorotate dehydrogenase B: electron transfer between two flavin groups bridged by an iron-sulphur cluster.
Rowland, P., Norager, S., Jensen, K.F., Larsen, S.(2000) Structure 8: 1227-1238
- PubMed: 11188687 
- DOI: https://doi.org/10.1016/s0969-2126(00)00530-x
- Primary Citation of Related Structures:  
1EP1, 1EP2, 1EP3 - PubMed Abstract: 
The fourth step and only redox reaction in pyrimidine de novo biosynthesis is catalyzed by the flavoprotein dihydroorotate dehydrogenase (DHOD). Based on their sequences, DHODs are grouped into two major families. Lactococcus lactis is one of the few organisms with two DHODs, A and B, belonging to each of the two subgroups of family 1. The B enzyme (DHODB) is a prototype for DHODs in Gram-positive bacteria that use NAD+ as the second substrate. DHODB is a heterotetramer composed of two different proteins (PyrDB and PyrK) and three different cofactors: FMN, FAD, and a [2Fe-2S] cluster.
Organizational Affiliation: 
Centre for Crystallographic Studies, Department of Chemistry, University of Copenhagen, Denmark.