4a57
From Proteopedia
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{{STRUCTURE_4a57| PDB=4a57 | SCENE= }} | {{STRUCTURE_4a57| PDB=4a57 | SCENE= }} | ||
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===CRYSTAL STRUCTURE OF TOXOPLASMA GONDII NUCLEOSIDE TRIPHOSPHATE DIPHOSPHOHYDROLASE 3 (NTPDASE3)=== | ===CRYSTAL STRUCTURE OF TOXOPLASMA GONDII NUCLEOSIDE TRIPHOSPHATE DIPHOSPHOHYDROLASE 3 (NTPDASE3)=== | ||
+ | {{ABSTRACT_PUBMED_22130673}} | ||
- | + | ==Function== | |
- | + | [[http://www.uniprot.org/uniprot/NTP1_TOXGO 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). | |
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==About this Structure== | ==About this Structure== | ||
- | [[4a57]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/ | + | [[4a57]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Toxgo Toxgo]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4A57 OCA]. |
==Reference== | ==Reference== | ||
- | <ref group="xtra">PMID:022130673</ref><references group="xtra"/> | + | <ref group="xtra">PMID:022130673</ref><references group="xtra"/><references/> |
[[Category: Nucleoside-triphosphatase]] | [[Category: Nucleoside-triphosphatase]] | ||
- | [[Category: | + | [[Category: Toxgo]] |
[[Category: Krug, U.]] | [[Category: Krug, U.]] | ||
[[Category: Straeter, N.]] | [[Category: Straeter, N.]] | ||
[[Category: Zebisch, M.]] | [[Category: Zebisch, M.]] | ||
[[Category: Hydrolase]] | [[Category: Hydrolase]] | ||
+ | [[Category: Ntpdase]] |
Revision as of 08:44, 25 December 2013
Contents |
CRYSTAL STRUCTURE OF TOXOPLASMA GONDII NUCLEOSIDE TRIPHOSPHATE DIPHOSPHOHYDROLASE 3 (NTPDASE3)
Template:ABSTRACT PUBMED 22130673
Function
[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 Structure
4a57 is a 4 chain structure with sequence from Toxgo. Full crystallographic information is available from OCA.
Reference
- 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