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| | <StructureSection load='4qxd' size='340' side='right'caption='[[4qxd]], [[Resolution|resolution]] 2.55Å' scene=''> | | <StructureSection load='4qxd' size='340' side='right'caption='[[4qxd]], [[Resolution|resolution]] 2.55Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4qxd]] is a 2 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4QXD FirstGlance]. <br> | + | <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> |
| - | </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> | + | </td></tr><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> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">EHI_179820 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=294381 Entamoeba histolytica HM-1:IMSS])</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=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> |
| - | <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>
| + | |
| - | <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://pdbe.org/4qxd PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4qxd RCSB], [http://www.ebi.ac.uk/pdbsum/4qxd PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4qxd ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/C4M633_ENTH1 C4M633_ENTH1] |
| | <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: Entamoeba histolytica hm-1:imss]] | + | [[Category: Entamoeba histolytica HM-1:IMSS]] |
| - | [[Category: Inositol-1,4-bisphosphate 1-phosphatase]]
| + | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Betzel, C]] | + | [[Category: Abdul Rehman SA]] |
| - | [[Category: Gourinath, S]] | + | [[Category: Betzel C]] |
| - | [[Category: Rehman, S A.Abdul]] | + | [[Category: Gourinath S]] |
| - | [[Category: Tarique, K F]] | + | [[Category: Tarique KF]] |
| - | [[Category: 1d-myo-inositol 1]]
| + | |
| - | [[Category: 1d-myo-inositol 4-phosphate]]
| + | |
| - | [[Category: 4-bisphosphate]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Hydrolysis]]
| + | |
| - | [[Category: Phosphate]]
| + | |
| Structural highlights
Function
C4M633_ENTH1
Publication Abstract from PubMed
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.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Faisal Tarique K, Arif Abdul Rehman S, Betzel C, Gourinath S. Structure-based identification of inositol polyphosphate 1-phosphatase from Entamoeba histolytica. Acta Crystallogr D Biol Crystallogr. 2014 Nov;70(Pt 11):3023-33. doi:, 10.1107/S1399004714021245. Epub 2014 Oct 29. PMID:25372691 doi:http://dx.doi.org/10.1107/S1399004714021245
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