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5cfj

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==Structural and functional attributes of malaria parasite Ap4A hydrolase==
==Structural and functional attributes of malaria parasite Ap4A hydrolase==
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<StructureSection load='5cfj' size='340' side='right' caption='[[5cfj]], [[Resolution|resolution]] 1.25&Aring;' scene=''>
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<StructureSection load='5cfj' size='340' side='right'caption='[[5cfj]], [[Resolution|resolution]] 1.25&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5cfj]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5CFJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5CFJ FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5cfj]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Plasmodium_falciparum_3D7 Plasmodium falciparum 3D7]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5CFJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5CFJ FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.25&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1xsc|1xsc]], [[5cfi|5cfi]]</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Bis(5'-nucleosyl)-tetraphosphatase_(asymmetrical) Bis(5'-nucleosyl)-tetraphosphatase (asymmetrical)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.1.17 3.6.1.17] </span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5cfj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5cfj OCA], [https://pdbe.org/5cfj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5cfj RCSB], [https://www.ebi.ac.uk/pdbsum/5cfj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5cfj ProSAT]</span></td></tr>
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<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=5cfj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5cfj OCA], [http://pdbe.org/5cfj PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5cfj RCSB], [http://www.ebi.ac.uk/pdbsum/5cfj PDBsum]</span></td></tr>
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</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/C0H4F3_PLAF7 C0H4F3_PLAF7]
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Malaria symptoms are driven by periodic multiplication cycles of Plasmodium parasites in human red blood corpuscles (RBCs). Malaria infection still accounts for ~600,000 annual deaths, and hence discovery of both new drug targets and drugs remains vital. In the present study, we have investigated the malaria parasite enzyme diadenosine tetraphosphate (Ap4A) hydrolase that regulates levels of signalling molecules like Ap4A by hydrolyzing them to ATP and AMP. We have tracked the spatial distribution of parasitic Ap4A hydrolase in infected RBCs, and reveal its unusual localization on the infected RBC membrane in subpopulation of infected cells. Interestingly, enzyme activity assays reveal an interaction between Ap4A hydrolase and the parasite growth inhibitor suramin. We also present a high resolution crystal structure of Ap4A hydrolase in apo- and sulphate- bound state, where the sulphate resides in the enzyme active site by mimicking the phosphate of substrates like Ap4A. The unexpected infected erythrocyte localization of the parasitic Ap4A hydrolase hints at a possible role of this enzyme in purinerigic signaling. In addition, atomic structure of Ap4A hydrolase provides insights for selective drug targeting.
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Structural and functional attributes of malaria parasite diadenosine tetraphosphate hydrolase.,Sharma A, Yogavel M, Sharma A Sci Rep. 2016 Feb 1;6:19981. doi: 10.1038/srep19981. PMID:26829485<ref>PMID:26829485</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 5cfj" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Sharma, A]]
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[[Category: Large Structures]]
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[[Category: Yogavel, M]]
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[[Category: Plasmodium falciparum 3D7]]
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[[Category: Ap4a]]
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[[Category: Sharma A]]
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[[Category: Hydrolase]]
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[[Category: Yogavel M]]
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[[Category: Nudix hydrolyse]]
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[[Category: Plasmodium]]
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[[Category: Purinergic signalling]]
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Current revision

Structural and functional attributes of malaria parasite Ap4A hydrolase

PDB ID 5cfj

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