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| ==Crystal structure of Staphylococcal inositol monophosphatase-1: 100 mM LiCl soaked inhibitory complex== | | ==Crystal structure of Staphylococcal inositol monophosphatase-1: 100 mM LiCl soaked inhibitory complex== |
| <StructureSection load='4i3y' size='340' side='right'caption='[[4i3y]], [[Resolution|resolution]] 2.04Å' scene=''> | | <StructureSection load='4i3y' size='340' side='right'caption='[[4i3y]]' scene=''> |
| == Structural highlights == | | == Structural highlights == |
| <table><tr><td colspan='2'>[[4i3y]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4I3Y OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4I3Y FirstGlance]. <br> | | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4I3Y OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4I3Y FirstGlance]. <br> |
| </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr> | | </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=4i3y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4i3y OCA], [https://pdbe.org/4i3y PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4i3y RCSB], [https://www.ebi.ac.uk/pdbsum/4i3y PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4i3y ProSAT]</span></td></tr> |
| <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3qmf|3qmf]], [[3ryd|3ryd]], [[4i40|4i40]], [[4ptk|4ptk]], [[4g61|4g61]]</div></td></tr>
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| <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Inositol-phosphate_phosphatase Inositol-phosphate phosphatase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.25 3.1.3.25] </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=4i3y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4i3y OCA], [https://pdbe.org/4i3y PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4i3y RCSB], [https://www.ebi.ac.uk/pdbsum/4i3y PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4i3y ProSAT]</span></td></tr> | |
| </table> | | </table> |
| <div style="background-color:#fffaf0;">
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| == Publication Abstract from PubMed ==
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| Mg2+ -dependent, Li+ -sensitive phosphatases are a widely distributed family of enzymes with significant importance throughout the biological kingdom. Inositol monophosphatase (IMPase) is one of the important targets of Li+ -based therapeutics for manic depressive disorders. However, despite decades of intense research efforts, the precise mechanism of the Li+ -induced inhibition of IMPase remains obscured. In this study, we present the structural investigation of the Li+ binding site in staphylococcal IMPase-I (SaIMPase-I) using X-ray crystallography. Biochemical study evident common or overlapping binding site of Mg2+ and Li+ in the active site of SaIMPase-I. The crystal structure of SaIMPase-I ternary product complex shows a phosphate and three Mg2+ (namely Mg1, Mg2 and Mg3) in the active site. Since Li+ is virtually invisible in X-ray crystallography, the competitive displacement of Mg2+ ions from the SaIMPase-I ternary product complex as a function of an increasing LiCl concentration were employed to identify Li+ binding site. In this approach, the disappearing electron density of pre-occupied Mg2+ ions due to Li+ ions binding was traced and accordingly, the Mg2+ ion explicitly from the Mg2 binding site found to be replaced. Moreover, based on comparative detailed investigation of the phosphate orientation and coordination states of Mg2+ binding sites in enzyme-substrate and enzyme-product complexes, the inhibition mechanisms of Li+ and Mg2+ are proposed. This article is protected by copyright. All rights reserved. STRUCTURED DIGITAL ABSTRACT: SaIMPase-I and SaIMPase-I bind by x-ray crystallography (View interaction).
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| Structural Elucidation of the Binding Site and Mode of Inhibition of Li and Mg in Inositol Monophosphatase.,Dutta A, Bhattacharyya S, Dutta D, Das AK FEBS J. 2014 Sep 26. doi: 10.1111/febs.13070. PMID:25263816<ref>PMID:25263816</ref>
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| From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| </div>
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| <div class="pdbe-citations 4i3y" style="background-color:#fffaf0;"></div>
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| ==See Also== | | ==See Also== |
| *[[Inositol monophosphatase 3D structures|Inositol monophosphatase 3D structures]] | | *[[Inositol monophosphatase 3D structures|Inositol monophosphatase 3D structures]] |
| == References ==
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| <references/>
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| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
| [[Category: Inositol-phosphate phosphatase]]
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| [[Category: Large Structures]] | | [[Category: Large Structures]] |
| [[Category: Bhattacharyya, S]] | | [[Category: Bhattacharyya S]] |
| [[Category: Das, A K]] | | [[Category: Das AK]] |
| [[Category: Dutta, A]] | | [[Category: Dutta A]] |
| [[Category: Dutta, D]] | | [[Category: Dutta D]] |
| [[Category: Cytoplasmic]]
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| [[Category: Hydrolase]]
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| [[Category: Inositol monophosphatase]]
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| [[Category: Magnesium binding]]
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| [[Category: Penta layer repeat of alpha/beta stretch]]
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