1OGL
The crystal structure of native Trypanosoma cruzi dUTPase
Summary for 1OGL
| Entry DOI | 10.2210/pdb1ogl/pdb |
| Related | 1OGK |
| Descriptor | DEOXYURIDINE TRIPHOSPHATASE (2 entities in total) |
| Functional Keywords | hydrolase, dutpase, trypanosoma cruzi, native, dimer |
| Biological source | TRYPANOSOMA CRUZI |
| Total number of polymer chains | 1 |
| Total formula weight | 32104.34 |
| Authors | Harkiolaki, M.,Dodson, E.J.,Bernier-Villamor, V.,Turkenburg, J.P.,Gonzalez-Pacanowska, D.,Wilson, K.S. (deposition date: 2003-05-07, release date: 2004-01-22, Last modification date: 2024-05-01) |
| Primary citation | Harkiolaki, M.,Dodson, E.J.,Bernier-Villamor, V.,Turkenburg, J.P.,Gonzalez-Pacanowska, D.,Wilson, K.S. The Crystal Structure of Trypanosoma Cruzi Dutpase Reveals a Novel Dutp/Dudp Binding Fold Structure, 12:41-, 2004 Cited by PubMed Abstract: dUTPase is an essential enzyme involved with nucleotide metabolism and replication. We report here the X-ray structure of Trypanosoma cruzi dUTPase in its native conformation and as a complex with dUDP. These reveal a novel protein fold that displays no structural similarities to previously described dUTPases. The molecular unit is a dimer with two active sites. Nucleotide binding promotes extensive structural rearrangements, secondary structure remodeling, and rigid body displacements of 20 A or more, which effectively bury the substrate within the enzyme core for the purpose of hydrolysis. The molecular complex is a trapped enzyme-substrate arrangement which clearly demonstrates structure-induced specificity and catalytic potential. This enzyme is a novel dUTPase and therefore a potential drug target in the treatment of Chagas' disease. PubMed: 14725764DOI: 10.1016/J.STR.2003.11.016 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.4 Å) |
Structure validation
Download full validation report
