2ibn: Difference between revisions

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New page: left|200px<br /> <applet load="2ibn" size="450" color="white" frame="true" align="right" spinBox="true" caption="2ibn, resolution 1.500Å" /> '''Crystal structure ...
 
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[[Image:2ibn.gif|left|200px]]<br />
<applet load="2ibn" size="450" color="white" frame="true" align="right" spinBox="true"
caption="2ibn, resolution 1.500&Aring;" />
'''Crystal structure of Human myo-Inositol Oxygenase (MIOX)'''<br />


==About this Structure==
==Crystal structure of Human myo-Inositol Oxygenase (MIOX)==
2IBN 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 FE, SO4, I1N and CYS as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Inositol_oxygenase Inositol oxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.13.99.1 1.13.99.1] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2IBN OCA].  
<StructureSection load='2ibn' size='340' side='right'caption='[[2ibn]], [[Resolution|resolution]] 1.50&Aring;' 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]] 1.5&#8491;</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/initialview03.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.
 
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>
 
From MEDLINE&reg;/PubMed&reg;, 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: Homo sapiens]]
[[Category: Inositol oxygenase]]
[[Category: Large Structures]]
[[Category: Single protein]]
[[Category: Arrowsmith C]]
[[Category: Arrowsmith, C.]]
[[Category: Berglund H]]
[[Category: Berg, S.Van.Den.]]
[[Category: Busam RD]]
[[Category: Berglund, H.]]
[[Category: Collins R]]
[[Category: Busam, R.D.]]
[[Category: Edwards A]]
[[Category: Collins, R.]]
[[Category: Ehn M]]
[[Category: Edwards, A.]]
[[Category: Flodin S]]
[[Category: Ehn, M.]]
[[Category: Flores A]]
[[Category: Flodin, S.]]
[[Category: Graslund S]]
[[Category: Flores, A.]]
[[Category: Hallberg BM]]
[[Category: Graslund, S.]]
[[Category: Hammarstrom M]]
[[Category: Hallberg, B.M.]]
[[Category: Hogbom M]]
[[Category: Hammarstrom, M.]]
[[Category: Holmberg-Schiavone L]]
[[Category: Hogbom, M.]]
[[Category: Johansson I]]
[[Category: Holmberg-Schiavone, L.]]
[[Category: Karlberg T]]
[[Category: Johansson, I.]]
[[Category: Kotenyova T]]
[[Category: Karlberg, T.]]
[[Category: Nilsson-Ehle P]]
[[Category: Kotenyova, T.]]
[[Category: Nordlund P]]
[[Category: Nilsson-Ehle, P.]]
[[Category: Nyman T]]
[[Category: Nordlund, P.]]
[[Category: Ogg D]]
[[Category: Nyman, T.]]
[[Category: Persson C]]
[[Category: Ogg, D.]]
[[Category: Sagemark J]]
[[Category: Persson, C.]]
[[Category: Stenmark P]]
[[Category: SGC, Structural.Genomics.Consortium.]]
[[Category: Sundstrom M]]
[[Category: Sagemark, J.]]
[[Category: Thorsell AG]]
[[Category: Stenmark, P.]]
[[Category: Uppenberg J]]
[[Category: Sundstrom, M.]]
[[Category: Van Den Berg S]]
[[Category: Thorsell, A.G.]]
[[Category: Weigelt J]]
[[Category: Uppenberg, J.]]
[[Category: Weigelt, J.]]
[[Category: CYS]]
[[Category: FE]]
[[Category: I1N]]
[[Category: SO4]]
[[Category: diiron]]
[[Category: inositol]]
[[Category: reductase]]
[[Category: sgc]]
[[Category: structural genomics]]
[[Category: structural genomics consortium]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 22:43:07 2007''

Latest revision as of 08:11, 30 October 2024

Crystal structure of Human myo-Inositol Oxygenase (MIOX)

2ibn, resolution 1.50Å

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