1JRB
The P56A mutant of Lactococcus lactis dihydroorotate dehydrogenase A
Summary for 1JRB
| Entry DOI | 10.2210/pdb1jrb/pdb |
| Related | 1DOR 1JQV 1JQX 1JRC 2DOR |
| Descriptor | dihydroorotate dehydrogenase A, FLAVIN MONONUCLEOTIDE, OROTIC ACID, ... (4 entities in total) |
| Functional Keywords | homodimer, alpha-beta barrel, flavoprotein, orotate complex, mutant enzyme, oxidoreductase |
| Biological source | Lactococcus lactis |
| Total number of polymer chains | 2 |
| Total formula weight | 69657.15 |
| Authors | Norager, S.,Arent, S.,Bjornberg, O.,Ottosen, M.,Lo Leggio, L.,Jensen, K.F.,Larsen, S. (deposition date: 2001-08-13, release date: 2003-09-09, Last modification date: 2023-10-25) |
| Primary citation | Norager, S.,Arent, S.,Bjornberg, O.,Ottosen, M.,Lo Leggio, L.,Jensen, K.F.,Larsen, S. Lactococcus lactis dihydroorotate dehydrogenase A mutants reveal important facets of the enzymatic function J.Biol.Chem., 278:28812-28822, 2003 Cited by PubMed Abstract: Dihydroorotate dehydrogenases (DHODs) are flavoenzymes catalyzing the oxidation of (S)-dihydroorotate to orotate in the biosynthesis of UMP, the precursor of all other pyrimidine nucleotides. On the basis of sequence, DHODs can be divided into two classes, class 1, further divided in subclasses 1A and 1B, and class 2. This division corresponds to differences in cellular location and the nature of the electron acceptor. Herein we report a study of Lactococcus lactis DHODA, a representative of the class 1A enzymes. Based on the DHODA structure we selected seven residues that are highly conserved between both main classes of DHODs as well as three residues representing surface charges close to the active site for site-directed mutagenesis. The availability of both kinetic and structural data on the mutant enzymes allowed us to define the roles individual structural segments play in catalysis. We have also structurally proven the presence of an open active site loop in DHODA and obtained information about the interactions that control movements of loops around the active site. Furthermore, in one mutant structure we observed differences between the two monomers of the dimer, confirming an apparent asymmetry between the two substrate binding sites that was indicated by the kinetic results. PubMed: 12732650DOI: 10.1074/jbc.M303767200 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
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