4jep
From Proteopedia
(Difference between revisions)
| Line 7: | Line 7: | ||
==About this Structure== | ==About this Structure== | ||
| - | [[4jep]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/ | + | [[4jep]] is a 2 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=4JEP OCA]. |
==Reference== | ==Reference== | ||
<ref group="xtra">PMID:023526564</ref><references group="xtra"/><references/> | <ref group="xtra">PMID:023526564</ref><references group="xtra"/><references/> | ||
[[Category: Nucleoside-triphosphatase]] | [[Category: Nucleoside-triphosphatase]] | ||
| - | [[Category: | + | [[Category: Toxgo]] |
[[Category: Krug, U.]] | [[Category: Krug, U.]] | ||
[[Category: Strater, N.]] | [[Category: Strater, N.]] | ||
[[Category: Totzauer, R.]] | [[Category: Totzauer, R.]] | ||
[[Category: Hydrolase]] | [[Category: Hydrolase]] | ||
| + | [[Category: Ntpdase]] | ||
[[Category: Phosphatase]] | [[Category: Phosphatase]] | ||
Revision as of 08:32, 25 December 2013
Contents |
Crystal structure of Toxoplasma gondii nucleoside triphosphate diphosphohydrolase 1 (NTPDase1)
Template:ABSTRACT PUBMED 23526564
Function
[NTP2_TOXGO] May perform an important processing step in the conversion of high energy nucleotides prior to uptake by the parasite. NTPAse-II has a specific activity 4.5-fold lower than NTPAse-I 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
4jep is a 2 chain structure with sequence from Toxgo. Full crystallographic information is available from OCA.
Reference
- Krug U, Totzauer R, Strater N. The crystal structure of Toxoplasma gondii nucleoside triphosphate diphosphohydrolase 1 represents a conformational intermediate in the reductive activation mechanism of the tetrameric enzyme. Proteins. 2013 Mar 22. doi: 10.1002/prot.24288. PMID:23526564 doi:10.1002/prot.24288
