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| | <StructureSection load='5wru' size='340' side='right'caption='[[5wru]], [[Resolution|resolution]] 3.19Å' scene=''> | | <StructureSection load='5wru' size='340' side='right'caption='[[5wru]], [[Resolution|resolution]] 3.19Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5wru]] is a 5 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5WRU OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5WRU FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5wru]] is a 5 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=5WRU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5WRU FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</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]] 3.193Å</td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5wrt|5wrt]]</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=5wru FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5wru OCA], [https://pdbe.org/5wru PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5wru RCSB], [https://www.ebi.ac.uk/pdbsum/5wru PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5wru ProSAT]</span></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Inorganic_diphosphatase Inorganic diphosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.1.1 3.6.1.1] </span></td></tr>
| + | |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5wru FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5wru OCA], [http://pdbe.org/5wru PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5wru RCSB], [http://www.ebi.ac.uk/pdbsum/5wru PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5wru ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/IPYR_PLAF7 IPYR_PLAF7] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Inorganic diphosphatase]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Jamwal, A]] | + | [[Category: Plasmodium falciparum 3D7]] |
| - | [[Category: Sharma, A]] | + | [[Category: Jamwal A]] |
| - | [[Category: Yogavel, M]] | + | [[Category: Sharma A]] |
| - | [[Category: Hydrolase]] | + | [[Category: Yogavel M]] |
| - | [[Category: Novel interface]]
| + | |
| - | [[Category: Ppase]]
| + | |
| - | [[Category: Ppi]]
| + | |
| Structural highlights
Function
IPYR_PLAF7
Publication Abstract from PubMed
Inorganic pyrophosphatases (PPase) participate in energy cycling and they are essential for growth and survival of organisms. Here we report extensive structural and functional characterization of soluble PPases from the human parasites Plasmodium falciparum (PfPPase) and Toxoplasma gondii (TgPPase). Our results show that PfPPase is a cytosolic enzyme whose gene expression is upregulated during parasite asexual stages. Cambialistic PfPPase actively hydrolyzes linear short chain polyphosphates like PPi, polyP3 and ATP in the presence of Zn2+. A remarkable new feature of PfPPase is the low complexity asparagine-rich N-terminal region that mediates its dimerization. Deletion of N-region has an unexpected and substantial effect on the stability of PfPPase domain, resulting in aggregation and significant loss of enzyme activity. Significantly, the crystal structures of PfPPase and TgPPase reveal unusual and unprecedented dimeric organizations and provide new fundamental insights into the variety of oligomeric assemblies possible in eukaryotic inorganic PPases.
Structural and Biochemical Characterization of Apicomplexan Inorganic Pyrophosphatases.,Jamwal A, Yogavel M, Abdin MZ, Jain SK, Sharma A Sci Rep. 2017 Jul 12;7(1):5255. doi: 10.1038/s41598-017-05234-y. PMID:28701714[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Jamwal A, Yogavel M, Abdin MZ, Jain SK, Sharma A. Structural and Biochemical Characterization of Apicomplexan Inorganic Pyrophosphatases. Sci Rep. 2017 Jul 12;7(1):5255. doi: 10.1038/s41598-017-05234-y. PMID:28701714 doi:http://dx.doi.org/10.1038/s41598-017-05234-y
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