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2ibn
From Proteopedia
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| - | [[Image:2ibn.gif|left|200px]]<br /><applet load="2ibn" size="350" color="white" frame="true" align="right" spinBox="true" | ||
| - | caption="2ibn, resolution 1.500Å" /> | ||
| - | '''Crystal structure of Human myo-Inositol Oxygenase (MIOX)'''<br /> | ||
| - | == | + | ==Crystal structure of Human myo-Inositol Oxygenase (MIOX)== |
| - | + | <StructureSection load='2ibn' size='340' side='right'caption='[[2ibn]], [[Resolution|resolution]] 1.50Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[2ibn]] 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=2IBN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2IBN 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]] 1.5Å</td></tr> | |
| - | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CYS:CYSTEINE'>CYS</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=I1N:(2S,3R,4R,5S,6S)-2,3,4,5,6-PENTAHYDROXYCYCLOHEXANONE'>I1N</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=2ibn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ibn OCA], [https://pdbe.org/2ibn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ibn RCSB], [https://www.ebi.ac.uk/pdbsum/2ibn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ibn ProSAT]</span></td></tr> | |
| - | + | </table> | |
| - | + | == Function == | |
| - | + | [https://www.uniprot.org/uniprot/MIOX_HUMAN MIOX_HUMAN] | |
| - | + | == Evolutionary Conservation == | |
| - | + | [[Image:Consurf_key_small.gif|200px|right]] | |
| - | + | Check<jmol> | |
| - | + | <jmolCheckbox> | |
| - | + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ib/2ibn_consurf.spt"</scriptWhenChecked> | |
| - | + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | |
| - | + | <text>to colour the structure by Evolutionary Conservation</text> | |
| - | + | </jmolCheckbox> | |
| - | + | </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=2ibn ConSurf]. | |
| - | + | <div style="clear:both"></div> | |
| - | + | <div style="background-color:#fffaf0;"> | |
| - | [ | + | == Publication Abstract from PubMed == |
| - | + | Altered inositol metabolism is implicated in a number of diabetic complications. The first committed step in mammalian inositol catabolism is performed by myo-inositol oxygenase (MIOX), which catalyzes a unique four-electron dioxygen-dependent ring cleavage of myo-inositol to D-glucuronate. Here, we present the crystal structure of human MIOX in complex with myo-inosose-1 bound in a terminal mode to the MIOX diiron cluster site. Furthermore, from biochemical and biophysical results from N-terminal deletion mutagenesis we show that the N terminus is important, through coordination of a set of loops covering the active site, in shielding the active site during catalysis. EPR spectroscopy of the unliganded enzyme displays a two-component spectrum that we can relate to an open and a closed active site conformation. Furthermore, based on site-directed mutagenesis in combination with biochemical and biophysical data, we propose a novel role for Lys(127) in governing access to the diiron cluster. | |
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| - | + | Structural and biophysical characterization of human myo-inositol oxygenase.,Thorsell AG, Persson C, Voevodskaya N, Busam RD, Hammarstrom M, Graslund S, Graslund A, Hallberg BM J Biol Chem. 2008 May 30;283(22):15209-16. Epub 2008 Mar 24. PMID:18364358<ref>PMID:18364358</ref> | |
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 2ibn" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Homo sapiens]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Arrowsmith C]] | ||
| + | [[Category: Berglund H]] | ||
| + | [[Category: Busam RD]] | ||
| + | [[Category: Collins R]] | ||
| + | [[Category: Edwards A]] | ||
| + | [[Category: Ehn M]] | ||
| + | [[Category: Flodin S]] | ||
| + | [[Category: Flores A]] | ||
| + | [[Category: Graslund S]] | ||
| + | [[Category: Hallberg BM]] | ||
| + | [[Category: Hammarstrom M]] | ||
| + | [[Category: Hogbom M]] | ||
| + | [[Category: Holmberg-Schiavone L]] | ||
| + | [[Category: Johansson I]] | ||
| + | [[Category: Karlberg T]] | ||
| + | [[Category: Kotenyova T]] | ||
| + | [[Category: Nilsson-Ehle P]] | ||
| + | [[Category: Nordlund P]] | ||
| + | [[Category: Nyman T]] | ||
| + | [[Category: Ogg D]] | ||
| + | [[Category: Persson C]] | ||
| + | [[Category: Sagemark J]] | ||
| + | [[Category: Stenmark P]] | ||
| + | [[Category: Sundstrom M]] | ||
| + | [[Category: Thorsell AG]] | ||
| + | [[Category: Uppenberg J]] | ||
| + | [[Category: Van Den Berg S]] | ||
| + | [[Category: Weigelt J]] | ||
Current revision
Crystal structure of Human myo-Inositol Oxygenase (MIOX)
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Categories: Homo sapiens | Large Structures | Arrowsmith C | Berglund H | Busam RD | Collins R | Edwards A | Ehn M | Flodin S | Flores A | Graslund S | Hallberg BM | Hammarstrom M | Hogbom M | Holmberg-Schiavone L | Johansson I | Karlberg T | Kotenyova T | Nilsson-Ehle P | Nordlund P | Nyman T | Ogg D | Persson C | Sagemark J | Stenmark P | Sundstrom M | Thorsell AG | Uppenberg J | Van Den Berg S | Weigelt J

