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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 1.500&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 <scene name='pdbligand=FE:'>FE</scene>, <scene name='pdbligand=SO4:'>SO4</scene>, <scene name='pdbligand=I1N:'>I1N</scene> and <scene name='pdbligand=CYS:'>CYS</scene> 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://oca.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://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:50:56 2008''

Latest revision as of 11:11, 30 October 2024

Crystal structure of Human myo-Inositol Oxygenase (MIOX)Crystal structure of Human myo-Inositol Oxygenase (MIOX)

Structural highlights

2ibn is a 2 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.5Å
Ligands:, , , ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

MIOX_HUMAN

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

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[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

  1. ↑ Thorsell AG, Persson C, Voevodskaya N, Busam RD, Hammarstrom M, Graslund S, Graslund A, Hallberg BM. Structural and biophysical characterization of human myo-inositol oxygenase. J Biol Chem. 2008 May 30;283(22):15209-16. Epub 2008 Mar 24. PMID:18364358 doi:10.1074/jbc.M800348200

2ibn, resolution 1.50Å

Drag the structure with the mouse to rotate

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OCA
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