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==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==
<StructureSection load='4a5a' size='340' side='right' caption='[[4a5a]], [[Resolution|resolution]] 2.85&Aring;' scene=''>
<StructureSection load='4a5a' size='340' side='right'caption='[[4a5a]], [[Resolution|resolution]] 2.85&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[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]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4A5A FirstGlance]. <br>
<table><tr><td colspan='2'>[[4a5a]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Toxoplasma_gondii Toxoplasma gondii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4A5A OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4A5A FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ANP:PHOSPHOAMINOPHOSPHONIC+ACID-ADENYLATE+ESTER'>ANP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.85&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4a57|4a57]], [[4a59|4a59]], [[4a5b|4a5b]]</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ANP:PHOSPHOAMINOPHOSPHONIC+ACID-ADENYLATE+ESTER'>ANP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Apyrase Apyrase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.1.5 3.6.1.5] </span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4a5a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4a5a OCA], [https://pdbe.org/4a5a PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4a5a RCSB], [https://www.ebi.ac.uk/pdbsum/4a5a PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4a5a ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4a5a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4a5a OCA], [http://pdbe.org/4a5a PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4a5a RCSB], [http://www.ebi.ac.uk/pdbsum/4a5a PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4a5a ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== 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).  
[https://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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<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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==See Also==
==See Also==
*[[Ectonucleoside triphosphate diphosphohydrolase|Ectonucleoside triphosphate diphosphohydrolase]]
*[[Ectonucleoside triphosphate diphosphohydrolase|Ectonucleoside triphosphate diphosphohydrolase]]
*[[Nucleoside triphosphatase|Nucleoside triphosphatase]]
*[[Sandbox 30008|Sandbox 30008]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Apyrase]]
[[Category: Large Structures]]
[[Category: Toxgo]]
[[Category: Toxoplasma gondii]]
[[Category: Krug, U]]
[[Category: Krug U]]
[[Category: Straeter, N]]
[[Category: Straeter N]]
[[Category: Zebisch, M]]
[[Category: Zebisch M]]
[[Category: Hydrolase]]
[[Category: Ntpdase]]

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