5wrt

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'''Unreleased structure'''
 
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The entry 5wrt is ON HOLD until Paper Publication
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==Crystal structure of type I inorganic pyrophosphatase from Toxoplasma gondii.==
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<StructureSection load='5wrt' size='340' side='right' caption='[[5wrt]], [[Resolution|resolution]] 2.35&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[5wrt]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5WRT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5WRT 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=MG:MAGNESIUM+ION'>MG</scene></td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5wru|5wru]]</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=5wrt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5wrt OCA], [http://pdbe.org/5wrt PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5wrt RCSB], [http://www.ebi.ac.uk/pdbsum/5wrt PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5wrt ProSAT]</span></td></tr>
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</table>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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Authors: Jamwal, A., Yogavel, M., Sharma, A.
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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<ref>PMID:28701714</ref>
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Description: Crystal structure of type I inorganic pyrophosphatase from Toxoplasma gondii.
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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[[Category: Yogavel, M]]
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<div class="pdbe-citations 5wrt" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
[[Category: Jamwal, A]]
[[Category: Jamwal, A]]
[[Category: Sharma, A]]
[[Category: Sharma, A]]
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[[Category: Yogavel, M]]
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[[Category: Hydrolase]]
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[[Category: Novel interface]]
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[[Category: Ppase]]
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[[Category: Ppi]]

Revision as of 06:58, 11 October 2017

Crystal structure of type I inorganic pyrophosphatase from Toxoplasma gondii.

5wrt, resolution 2.35Å

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