3oix
From Proteopedia
Crystal structure of the putative dihydroorotate dehydrogenase from Streptococcus mutans
Structural highlights
FunctionQ8DVA1_STRMU Catalyzes the conversion of dihydroorotate to orotate (By similarity).[HAMAP-Rule:MF_00224] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedStreptococcus 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 A 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. Structure of the putative dihydroorotate dehydrogenase from Streptococcus mutans.,Liu Y, Gao ZQ, Liu CP, Xu JH, Li LF, Ji CN, Su XD, Dong YH Acta Crystallogr Sect F Struct Biol Cryst Commun. 2011 Feb 1;67(Pt, 2):182-7. Epub 2011 Jan 21. PMID:21301083[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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