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4qxd

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==Crystal structure of Inositol Polyphosphate 1-Phosphatase from Entamoeba histolytica==
==Crystal structure of Inositol Polyphosphate 1-Phosphatase from Entamoeba histolytica==
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<StructureSection load='4qxd' size='340' side='right' caption='[[4qxd]], [[Resolution|resolution]] 2.55&Aring;' scene=''>
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<StructureSection load='4qxd' size='340' side='right'caption='[[4qxd]], [[Resolution|resolution]] 2.55&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4qxd]] is a 2 chain structure. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=4j13 4j13]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4QXD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4QXD FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4qxd]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Entamoeba_histolytica_HM-1:IMSS Entamoeba histolytica HM-1:IMSS]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=4j13 4j13]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4QXD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4QXD 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>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</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]] 2.55&#8491;</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/Inositol-1,4-bisphosphate_1-phosphatase Inositol-1,4-bisphosphate 1-phosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.57 3.1.3.57] </span></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=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></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=4qxd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4qxd OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4qxd RCSB], [http://www.ebi.ac.uk/pdbsum/4qxd PDBsum]</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=4qxd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4qxd OCA], [https://pdbe.org/4qxd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4qxd RCSB], [https://www.ebi.ac.uk/pdbsum/4qxd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4qxd ProSAT]</span></td></tr>
</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/C4M633_ENTH1 C4M633_ENTH1]
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Inositol polyphosphate 1-phosphatase from Entamoeba histolytica (EhIPPase) is an Mg(2+)-dependent and Li(+)-sensitive enzyme that catalyzes the hydrolysis of inositol 1,4-bisphosphate [Ins(1,4)P2] into myo-inositol 1-monophosphate and PO4(3-). In the present work, EhIPPase has been biochemically identified and its crystal structure has been determined in the presence of Mg(2+) and PO4(3-) at 2.5 A resolution. This enzyme was previously classified as a 3'(2'),5'-bisphosphate nucleotidase in the NCBI, but its biochemical activity and structural analysis suggest that this enzyme behaves more like an inositol polyphosphate 1-phosphatase. The ability of EhIPPase to hydrolyze the smaller Ins(1,4)P2 better than the bulkier 3'-phosphoadenosine 5'-phosphate (PAP) is explained on the basis of the orientations of amino-acid residues in the binding site. This structure is the first of its class to be determined from any protozoan parasite, and is the third to determined among all organisms, following its rat and bovine homologues. The three-dimensional fold of EhIPPase is similar to those of other members of the inositol monophosphatase superfamily, which also includes inositol monophosphatase, 3'(2'),5'-bisphosphate nucleotidase and fructose-1,6-bisphosphate 1-phosphatase. They all share conserved residues essential for metal binding and substrate hydrolysis, with the motif D-Xn-EE-Xn-DP(I/L)DG(S/T)-Xn-WD-Xn-GG. The structure is divided into two domains, namely alpha+beta and alpha/beta, and the substrate and metal ions bind between them. However, the ability of each enzyme class to act specifically on its cognate substrate is governed by the class-specific amino-acid residues at the active site.
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Structure-based identification of inositol polyphosphate 1-phosphatase from Entamoeba histolytica.,Faisal Tarique K, Arif Abdul Rehman S, Betzel C, Gourinath S Acta Crystallogr D Biol Crystallogr. 2014 Nov;70(Pt 11):3023-33. doi:, 10.1107/S1399004714021245. Epub 2014 Oct 29. PMID:25372691<ref>PMID:25372691</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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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Inositol-1,4-bisphosphate 1-phosphatase]]
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[[Category: Entamoeba histolytica HM-1:IMSS]]
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[[Category: Betzel, C]]
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[[Category: Large Structures]]
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[[Category: Gourinath, S]]
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[[Category: Abdul Rehman SA]]
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[[Category: Rehman, S A.Abdul]]
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[[Category: Betzel C]]
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[[Category: Tarique, K F]]
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[[Category: Gourinath S]]
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[[Category: 1d-myo-inositol 1]]
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[[Category: Tarique KF]]
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[[Category: 1d-myo-inositol 4-phosphate]]
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[[Category: 4-bisphosphate]]
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[[Category: Hydrolase]]
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[[Category: Hydrolysis]]
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[[Category: Phosphate]]
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Current revision

Crystal structure of Inositol Polyphosphate 1-Phosphatase from Entamoeba histolytica

PDB ID 4qxd

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