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==Crystal Structure of IMPase/NADP phosphatase complexed with NADP and Ca2+ at pH 7.0== | ==Crystal Structure of IMPase/NADP phosphatase complexed with NADP and Ca2+ at pH 7.0== | ||
<StructureSection load='5eyh' size='340' side='right' caption='[[5eyh]], [[Resolution|resolution]] 2.50Å' scene=''> | <StructureSection load='5eyh' size='340' side='right' caption='[[5eyh]], [[Resolution|resolution]] 2.50Å' scene=''> | ||
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5eyg|5eyg]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5eyg|5eyg]]</td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Inositol-phosphate_phosphatase Inositol-phosphate phosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.25 3.1.3.25] </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-phosphate_phosphatase Inositol-phosphate phosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.25 3.1.3.25] </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=5eyh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5eyh OCA], [http://pdbe.org/5eyh PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5eyh RCSB], [http://www.ebi.ac.uk/pdbsum/5eyh PDBsum]</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=5eyh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5eyh OCA], [http://pdbe.org/5eyh PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5eyh RCSB], [http://www.ebi.ac.uk/pdbsum/5eyh PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5eyh ProSAT]</span></td></tr> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
NADP(H)/NAD(H) homeostasis has long been identified to play a pivotal role in the mitigation of reactive oxygen stress (ROS) in the intracellular milieu and is therefore critical for the progression and pathogenesis of many diseases. NAD(H) kinases and NADP(H) phosphatases are two key players in this pathway. Despite structural evidence demonstrating the existence and mode of action of NAD(H) kinases, the specific annotation and the mode of action of NADP(H) phosphatases remains obscure. Here, structural evidence supporting the alternative role of inositol monophosphatase (IMPase) as an NADP(H) phosphatase is reported. Crystal structures of staphylococcal dual-specific IMPase/NADP(H) phosphatase (SaIMPase-I) in complex with the substrates D-myo-inositol-1-phosphate and NADP(+) have been solved. The structure of the SaIMPase-I-Ca(2+)-NADP(+) ternary complex reveals the catalytic mode of action of NADP(H) phosphatase. Moreover, structures of SaIMPase-I-Ca(2+)-substrate complexes have reinforced the earlier proposal that the length of the active-site-distant helix alpha4 and its preceding loop are the predisposing factors for the promiscuous substrate specificity of SaIMPase-I. Altogether, the evidence presented suggests that IMPase-family enzymes with a shorter alpha4 helix could be potential candidates for previously unreported NADP(H) phosphatase activity. | |||
Structural elucidation of the NADP(H) phosphatase activity of staphylococcal dual-specific IMPase/NADP(H) phosphatase.,Bhattacharyya S, Dutta A, Dutta D, Ghosh AK, Das AK Acta Crystallogr D Struct Biol. 2016 Feb;72(Pt 2):281-90. doi:, 10.1107/S2059798316000620. Epub 2016 Jan 28. PMID:26894675<ref>PMID:26894675</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 5eyh" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Inositol Monophosphatase|Inositol Monophosphatase]] | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Revision as of 19:28, 25 January 2017
Crystal Structure of IMPase/NADP phosphatase complexed with NADP and Ca2+ at pH 7.0Crystal Structure of IMPase/NADP phosphatase complexed with NADP and Ca2+ at pH 7.0
Structural highlights
Publication Abstract from PubMedNADP(H)/NAD(H) homeostasis has long been identified to play a pivotal role in the mitigation of reactive oxygen stress (ROS) in the intracellular milieu and is therefore critical for the progression and pathogenesis of many diseases. NAD(H) kinases and NADP(H) phosphatases are two key players in this pathway. Despite structural evidence demonstrating the existence and mode of action of NAD(H) kinases, the specific annotation and the mode of action of NADP(H) phosphatases remains obscure. Here, structural evidence supporting the alternative role of inositol monophosphatase (IMPase) as an NADP(H) phosphatase is reported. Crystal structures of staphylococcal dual-specific IMPase/NADP(H) phosphatase (SaIMPase-I) in complex with the substrates D-myo-inositol-1-phosphate and NADP(+) have been solved. The structure of the SaIMPase-I-Ca(2+)-NADP(+) ternary complex reveals the catalytic mode of action of NADP(H) phosphatase. Moreover, structures of SaIMPase-I-Ca(2+)-substrate complexes have reinforced the earlier proposal that the length of the active-site-distant helix alpha4 and its preceding loop are the predisposing factors for the promiscuous substrate specificity of SaIMPase-I. Altogether, the evidence presented suggests that IMPase-family enzymes with a shorter alpha4 helix could be potential candidates for previously unreported NADP(H) phosphatase activity. Structural elucidation of the NADP(H) phosphatase activity of staphylococcal dual-specific IMPase/NADP(H) phosphatase.,Bhattacharyya S, Dutta A, Dutta D, Ghosh AK, Das AK Acta Crystallogr D Struct Biol. 2016 Feb;72(Pt 2):281-90. doi:, 10.1107/S2059798316000620. Epub 2016 Jan 28. PMID:26894675[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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