1OGK

The crystal structure of Trypanosoma cruzi dUTPase in complex with dUDP

Summary for 1OGK

• Entry DOI: 10.2210/pdb1ogk/pdb
• Related: 1OGL
• Descriptor: DEOXYURIDINE TRIPHOSPHATASE, DEOXYURIDINE-5'-DIPHOSPHATE (2 entities in total)
• Functional Keywords: dimer, hydrolase
• Biological source: TRYPANOSOMA CRUZI
• Total number of polymer chains: 4
• Total formula weight: 129581.85

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

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: 14725764
DOI: 10.1016/J.STR.2003.11.016

Experimental method

X-RAY DIFFRACTION (2.85 Å)