3OIX

Crystal structure of the putative dihydroorotate dehydrogenase from Streptococcus mutans

Summary for 3OIX

• Entry DOI: 10.2210/pdb3oix/pdb
• Descriptor: Putative dihydroorotate dehydrogenase; dihydroorotate oxidase, FLAVIN MONONUCLEOTIDE, GLYCEROL, ... (4 entities in total)
• Functional Keywords: tim barrel, oxidoreductase
• Biological source: Streptococcus mutans
• Cellular location: Cytoplasm : Q8DVA1
• Total number of polymer chains: 4
• Total formula weight: 154074.78

Authors

Liu, Y.,Gao, Z.Q.,Liu, C.P.,Dong, Y.H. (deposition date: 2010-08-20, release date: 2010-09-08, Last modification date: 2023-11-01)

Primary citation

Liu, Y.,Gao, Z.-Q.,Liu, C.-P.,Xu, J.-H.,Li, L.-F.,Ji, C.-N.,Su, X.-D.,Dong, Y.-H.
Structure of the putative dihydroorotate dehydrogenase from Streptococcus mutans
Acta Crystallogr.,Sect.F, 67:182-187, 2011

PubMed Abstract: Streptococcus mutans is one of the pathogenic species involved in dental caries, especially in the initiation and development stages. Here, the crystal structure of SMU.595, a putative dihydroorotate dehydrogenase (DHOD) from S. mutans, is reported at 2.4 Å resolution. DHOD is a flavin mononucleotide-containing enzyme which catalyzes the oxidation of L-dihydroorotate to orotate, which is the fourth step and the only redox reaction in the de novo biosynthesis of pyrimidine nucleotides. The reductive lysine-methylation procedure was applied in order to improve the diffraction qualities of the crystals. Analysis of the S. mutans DHOD crystal structure shows that this enzyme is a class 1A DHOD and also suggests potential sites that could be exploited for the design of highly specific inhibitors using the structure-based chemotherapeutic design technique.

PubMed: 21301083
DOI: 10.1107/S1744309110048414

Experimental method

X-RAY DIFFRACTION (2.399 Å)