4a5a: Difference between revisions
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{{STRUCTURE_4a5a| PDB=4a5a | SCENE= }} | {{STRUCTURE_4a5a| PDB=4a5a | SCENE= }} | ||
===Crystal structure of the C258S/C268S variant of Toxoplasma gondii nucleoside triphosphate diphosphohydrolase 3 (NTPDase3) in complex with magnesium and AMPPNP=== | ===Crystal structure of the C258S/C268S variant of Toxoplasma gondii nucleoside triphosphate diphosphohydrolase 3 (NTPDase3) in complex with magnesium and AMPPNP=== | ||
{{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== | ||
[[4a5a]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/ | [[4a5a]] 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=4A5A OCA]. | ||
==Reference== | ==Reference== | ||
<ref group="xtra">PMID:022130673</ref><references group="xtra"/> | <ref group="xtra">PMID:022130673</ref><references group="xtra"/><references/> | ||
[[Category: Apyrase]] | [[Category: Apyrase]] | ||
[[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 08:52, 25 December 2013
Crystal structure of the C258S/C268S variant of Toxoplasma gondii nucleoside triphosphate diphosphohydrolase 3 (NTPDase3) in complex with magnesium and AMPPNP
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
4a5a 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
