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''' | ==Crystal structure of Staphylococcal IMPase-I complex with 3Mg2+ and Phosphate== | ||
<StructureSection load='4ptk' size='340' side='right' caption='[[4ptk]], [[Resolution|resolution]] 2.50Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4ptk]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4PTK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4PTK FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr> | |||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4g61|4g61]], [[4i3y|4i3y]], [[4i40|4i40]]</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=4ptk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ptk OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4ptk RCSB], [http://www.ebi.ac.uk/pdbsum/4ptk PDBsum]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
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). | |||
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> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Bhattacharyya, S.]] | |||
[[Category: Das, A K.]] | |||
[[Category: Dutta, A.]] | |||
[[Category: Dutta, D.]] | |||
[[Category: Hydrolase]] | |||
[[Category: Impase product complex]] | |||
Revision as of 11:43, 22 October 2014
Crystal structure of Staphylococcal IMPase-I complex with 3Mg2+ and Phosphate
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