1EP3

CRYSTAL STRUCTURE OF LACTOCOCCUS LACTIS DIHYDROOROTATE DEHYDROGENASE B. DATA COLLECTED UNDER CRYOGENIC CONDITIONS.

Summary for 1EP3

• Entry DOI: 10.2210/pdb1ep3/pdb
• Related: 1EP1 1EP2
• Descriptor: DIHYDROOROTATE DEHYDROGENASE B (PYRD SUBUNIT), DIHYDROOROTATE DEHYDROGENASE B (PYRK SUBUNIT), FLAVIN MONONUCLEOTIDE, ... (6 entities in total)
• Functional Keywords: heterotetramer, alpha-beta barrel, beta sandwich, fad domain, alpha/beta nadp domain, fes cluster binding domain, oxidoreductase
• Biological source: Lactococcus lactis; More
• Cellular location: Cytoplasm: P54322 P56968
• Total number of polymer chains: 2
• Total formula weight: 63085.30

Authors

Rowland, P.,Norager, S.,Jensen, K.F.,Larsen, S. (deposition date: 2000-03-27, release date: 2001-01-17, Last modification date: 2023-08-09)

Primary citation

Rowland, P.,Norager, S.,Jensen, K.F.,Larsen, S.
Structure of dihydroorotate dehydrogenase B: electron transfer between two flavin groups bridged by an iron-sulphur cluster.
Structure Fold.Des., 8:1227-1238, 2000

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.

PubMed: 11188687
DOI: 10.1016/S0969-2126(00)00530-X

Experimental method

X-RAY DIFFRACTION (2.1 Å)