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1imc

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[[Image:1imc.jpg|left|200px]]<br /><applet load="1imc" size="350" color="white" frame="true" align="right" spinBox="true"
 
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caption="1imc, resolution 2.60&Aring;" />
 
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'''STRUCTURAL STUDIES OF METAL BINDING BY INOSITOL MONOPHOSPHATASE: EVIDENCE FOR TWO-METAL ION CATALYSIS'''<br />
 
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==Overview==
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==STRUCTURAL STUDIES OF METAL BINDING BY INOSITOL MONOPHOSPHATASE: EVIDENCE FOR TWO-METAL ION CATALYSIS==
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The structure of inositol monophosphatase has been determined to 2.60 A, resolution in complexes with Mn2+ and with Mn2+ and phosphate. In the Mn2+, complex, three metal cations and one Cl were bound in the active site on, each of the two subunits of the enzyme. Ligands to the three metals, include the side chains of Glu 70, Asp 90, Asp 93, and Asp 220, t he, carbonyl group of Ile 92, several solvent molecules and the chloride, which is a ligand to each of the cations. When phosphate is soaked into, these Mn2+ cocrystals, one of the three Mn2+ ions is expelled from the, active site, leaving metal ions with octahedral and tetrahedral, coordination geometry. In addition, the structure of apoinositol, monophosphatase was determined to 2.5 A resolution. Residues 70-75, a, two-turn helical segment which is involved in metal coordination, moves, away from the metal binding site by 2-3 A in the absence of cations., Residues 30-40, which wrap around the metal binding site and interact with, the metal indirectly through solvent molecules and protein ligands to the, metal, become disordered in the absence of metal. In various metal, complexes, segmental mobility is also observed in the residues which form, the metal binding sites. The results of these studies of the interaction, of inositol monophosphatase with cations suggest that the enzyme, accomplishes phosphate ester hydrolysis using two metal ions, one with, octahedral and one with tetrahedral coordination geometry. Broad, metal-binding specificity appears to result from extensive flexibility in, several of the protein segments which contribute metal ligands, from the, presence of alternate metal ligands and from metal coordination spheres, which include water molecules.
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<StructureSection load='1imc' size='340' side='right'caption='[[1imc]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1imc]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IMC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1IMC FirstGlance]. <br>
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</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>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene></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=1imc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1imc OCA], [https://pdbe.org/1imc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1imc RCSB], [https://www.ebi.ac.uk/pdbsum/1imc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1imc ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/IMPA1_HUMAN IMPA1_HUMAN] Responsible for the provision of inositol required for synthesis of phosphatidylinositol and polyphosphoinositides and has been implicated as the pharmacological target for lithium action in brain. Can use myo-inositol monophosphates, myo-inositol 1,3-diphosphate, myo-inositol 1,4-diphosphate, scyllo-inositol-phosphate, glucose-1-phosphate, glucose-6-phosphate, fructose-1-phosphate, beta-glycerophosphate, and 2'-AMP as substrates.<ref>PMID:17068342</ref>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/im/1imc_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1imc ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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1IMC is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=MN:'>MN</scene> and <scene name='pdbligand=CL:'>CL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IMC OCA].
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*[[Inositol monophosphatase 3D structures|Inositol monophosphatase 3D structures]]
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== References ==
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==Reference==
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<references/>
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Structural studies of metal binding by inositol monophosphatase: evidence for two-metal ion catalysis., Bone R, Frank L, Springer JP, Atack JR, Biochemistry. 1994 Aug 16;33(32):9468-76. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8068621 8068621]
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__TOC__
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</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Inositol-phosphate phosphatase]]
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[[Category: Large Structures]]
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[[Category: Single protein]]
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[[Category: Bone R]]
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[[Category: Bone, R.]]
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[[Category: CL]]
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[[Category: MN]]
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[[Category: hydrolase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 16:02:22 2008''
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Current revision

STRUCTURAL STUDIES OF METAL BINDING BY INOSITOL MONOPHOSPHATASE: EVIDENCE FOR TWO-METAL ION CATALYSIS

PDB ID 1imc

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