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| | ==Crystal structure of 3'(2'),5'-bisphosphate nucleotidase1 from Entamoeba histolytica in complex with AMP and metal ions== | | ==Crystal structure of 3'(2'),5'-bisphosphate nucleotidase1 from Entamoeba histolytica in complex with AMP and metal ions== |
| - | <StructureSection load='4hxv' size='340' side='right' caption='[[4hxv]], [[Resolution|resolution]] 2.60Å' scene=''> | + | <StructureSection load='4hxv' size='340' side='right'caption='[[4hxv]], [[Resolution|resolution]] 2.60Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4hxv]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Enthi Enthi]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4HXV OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4HXV FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4hxv]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Entamoeba_histolytica Entamoeba histolytica]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4HXV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4HXV FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=AMP:ADENOSINE+MONOPHOSPHATE'>AMP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AMP:ADENOSINE+MONOPHOSPHATE'>AMP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">EHI_193350 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=5759 ENTHI])</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=4hxv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4hxv OCA], [https://pdbe.org/4hxv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4hxv RCSB], [https://www.ebi.ac.uk/pdbsum/4hxv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4hxv 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/3'(2'),5'-bisphosphate_nucleotidase 3'(2'),5'-bisphosphate nucleotidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.7 3.1.3.7] </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=4hxv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4hxv OCA], [http://pdbe.org/4hxv PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4hxv RCSB], [http://www.ebi.ac.uk/pdbsum/4hxv PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4hxv ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/C4M4T9_ENTHI C4M4T9_ENTHI] |
| | <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: Enthi]] | + | [[Category: Entamoeba histolytica]] |
| - | [[Category: Gourinath, S]] | + | [[Category: Large Structures]] |
| - | [[Category: Rehman, S A.Abdul]] | + | [[Category: Abdul Rehman SA]] |
| - | [[Category: Tarique, K F]] | + | [[Category: Gourinath S]] |
| - | [[Category: Adenosine 3s']] | + | [[Category: Tarique KF]] |
| - | [[Category: Dephosphorylation]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Hydrolysis]]
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| Structural highlights
Function
C4M4T9_ENTHI
Publication Abstract from PubMed
The enzyme 3'-phosphoadenosine 5'-phosphatase-1 (PAP phosphatase-1) is a member of the Li(+)-sensitive Mg(2+)-dependent phosphatase superfamily, or inositol monophosphatase (IMPase) superfamily, and is an important regulator of the sulfate-activation pathway in all living organisms. Inhibition of this enzyme leads to accumulation of the toxic byproduct 3'-phosphoadenosine 5'-phosphate (PAP), which could be lethal to the organism. Genomic analysis of Entamoeba histolytica suggests the presence of two isoforms of PAP phosphatase. The PAP phosphatase-1 isoform of this organism is shown to be active over wide ranges of pH and temperature. Interestingly, this enzyme is inhibited by submillimolar concentrations of Li(+), while being insensitive to Na(+). Interestingly, the enzyme showed activity towards both PAP and inositol 1,4-bisphosphate and behaved as an inositol polyphosphate 1-phosphatase. Crystal structures of this enzyme in its native form and in complex with adenosine 5'-monophosphate have been determined to 2.1 and 2.6 A resolution, respectively. The PAP phosphatase-1 structure is divided into two domains, namely alpha+beta and alpha/beta, and the substrate and metal ions bind between them. This is a first structure of any PAP phosphatase to be determined from a human parasitic protozoan. This enzyme appears to function using a mechanism involving three-metal-ion assisted catalysis. Comparison with other structures indicates that the sensitivity to alkali-metal ions may depend on the orientation of a specific catalytic loop.
Structural elucidation of a dual-activity PAP phosphatase-1 from Entamoeba histolytica capable of hydrolysing both 3'-phosphoadenosine 5'-phosphate and inositol 1,4-bisphosphate.,Faisal Tarique K, Arif Abdul Rehman S, Gourinath S Acta Crystallogr D Biol Crystallogr. 2014 Jul 1;70(Pt 7):2019-31. doi:, 10.1107/S1399004714010268. Epub 2014 Jun 29. PMID:25004978[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Faisal Tarique K, Arif Abdul Rehman S, Gourinath S. Structural elucidation of a dual-activity PAP phosphatase-1 from Entamoeba histolytica capable of hydrolysing both 3'-phosphoadenosine 5'-phosphate and inositol 1,4-bisphosphate. Acta Crystallogr D Biol Crystallogr. 2014 Jul 1;70(Pt 7):2019-31. doi:, 10.1107/S1399004714010268. Epub 2014 Jun 29. PMID:25004978 doi:http://dx.doi.org/10.1107/S1399004714010268
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