View source for 4hxv


==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]] 2.60&Aring;' scene=''>
== Structural highlights ==
<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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.6&#8491;</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='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>
</table>
== Function ==
[https://www.uniprot.org/uniprot/C4M4T9_ENTHI C4M4T9_ENTHI] 
<div style="background-color:#fffaf0;">
== 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<ref>PMID:25004978</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4hxv" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Entamoeba histolytica]]
[[Category: Large Structures]]
[[Category: Abdul Rehman SA]]
[[Category: Gourinath S]]
[[Category: Tarique KF]]