3C3N
Crystal structure of dihydroorotate dehydrogenase from Trypanosoma cruzi strain Y
Summary for 3C3N
Entry DOI | 10.2210/pdb3c3n/pdb |
Descriptor | Dihydroorotate dehydrogenase, SULFATE ION, FLAVIN MONONUCLEOTIDE, ... (5 entities in total) |
Functional Keywords | dhodh, trypanosoma cruzi strain y, dihydroorotate dehydrogenase, pyrd, oxidoreductase |
Biological source | Trypanosoma cruzi |
Cellular location | Cytoplasm (By similarity): Q4D3W2 |
Total number of polymer chains | 4 |
Total formula weight | 138222.10 |
Authors | Pinheiro, M.P.,Iulek, J.,Nonato, M.C. (deposition date: 2008-01-28, release date: 2008-04-29, Last modification date: 2024-02-21) |
Primary citation | Pinheiro, M.P.,Iulek, J.,Cristina Nonato, M. Crystal structure of Trypanosoma cruzi dihydroorotate dehydrogenase from Y strain Biochem.Biophys.Res.Commun., 369:812-817, 2008 Cited by PubMed Abstract: Trypanosoma cruzi is the etiological agent of Chagas' disease, a pathogenesis that affects millions of people in Latin America. Here, we report the crystal structure of dihydroorotate dehydrogenase (DHODH) from T. cruzi strain Y solved at 2.2A resolution. DHODH is a flavin mononucleotide containing enzyme, which catalyses the oxidation of l-dihydroorotate to orotate, the fourth step and only redox reaction in the de novo biosynthesis of pyrimidine nucleotides. Genetic studies have shown that DHODH is essential for T. cruzi survival, validating the idea that this enzyme can be considered an attractive target for the development of antichagasic drugs. In our work, a detailed analysis of T. cruzi DHODH crystal structure has allowed us to suggest potential sites to be further exploited for the design of highly specific inhibitors through the technology of structure-based drug design. PubMed: 18302934DOI: 10.1016/j.bbrc.2008.02.074 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.2 Å) |
Structure validation
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