4a59
Crystal structure of Toxoplasma gondii nucleoside triphosphate diphosphohydrolase 3 (NTPDase3) in complex with AMPCrystal structure of Toxoplasma gondii nucleoside triphosphate diphosphohydrolase 3 (NTPDase3) in complex with AMP
FunctionFunction
[NTP1_TOXGO] May perform an important processing step in the conversion of high energy nucleotides prior to uptake by the parasite and may contribute to intracellular survival and virulence. NTPAse-I has a specific activity 4.5-fold higher than NTPAse-II in hydrolysis of ATP. The primary difference between these isozymes lies in their ability to hydrolyze nucleoside triphosphate versus diphosphate substrates. While NTPAse-II hydrolyzes ATP to ADP and ADP to AMP at almost the same rate, NTPAse-I hydrolyzes ADP to AMP at a much slower rate (0.7% of the rate for ATP).
About this StructureAbout this Structure
4a59 is a 4 chain structure with sequence from Toxgo. Full crystallographic information is available from OCA.
ReferenceReference
- ↑ Krug U, Zebisch M, Krauss M, Strater N. Structural insight into the activation mechanism of Toxoplasma gondii nucleoside triphosphate diphosphohydrolases by disulfide reduction. J Biol Chem. 2011 Nov 30. PMID:22130673 doi:10.1074/jbc.M111.294348