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2huo

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(New page: 200px<br /><applet load="2huo" size="450" color="white" frame="true" align="right" spinBox="true" caption="2huo, resolution 2.00&Aring;" /> '''Crystal structure of...)
Current revision (09:34, 14 February 2024) (edit) (undo)
 
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[[Image:2huo.gif|left|200px]]<br /><applet load="2huo" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="2huo, resolution 2.00&Aring;" />
 
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'''Crystal structure of mouse myo-inositol oxygenase in complex with substrate'''<br />
 
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==Overview==
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==Crystal structure of mouse myo-inositol oxygenase in complex with substrate==
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Altered metabolism of the inositol sugars myo-inositol (MI) and, d-chiro-inositol is implicated in diabetic complications. In animals, catabolism of MI and D-chiro-inositol depends on the enzyme MI oxygenase, (MIOX), which catalyzes the first committed step of the, glucuronate-xylulose pathway, and is found almost exclusively in the, kidneys. The crystal structure of MIOX, in complex with MI, has been, determined by multiwavelength anomalous diffraction methods and refined at, 2.0-A resolution (R=0.206, Rfree=0.253). The structure reveals a, monomeric, single-domain protein with a mostly helical fold that is, distantly related to the diverse HD domain superfamily. Five helices form, the structural core and provide six ligands (four His and two Asp) for the, di-iron center, in which the two iron atoms are bridged by a putative, hydroxide ion and one of the Asp ligands, Asp-124. A key loop forms a lid, over the MI substrate, which is coordinated in bidentate mode to one iron, atom. It is proposed that this mode of iron coordination, and interaction, with a key Lys residue, activate MI for bond cleavage. The structure also, reveals the basis of substrate specificity and suggests routes for the, development of specific MIOX inhibitors.
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<StructureSection load='2huo' size='340' side='right'caption='[[2huo]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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== Structural highlights ==
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==About this Structure==
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<table><tr><td colspan='2'>[[2huo]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HUO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2HUO FirstGlance]. <br>
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2HUO is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with FE, OH, INS and FMT 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=2HUO OCA].
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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&#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=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=FMT:FORMIC+ACID'>FMT</scene>, <scene name='pdbligand=INS:1,2,3,4,5,6-HEXAHYDROXY-CYCLOHEXANE'>INS</scene>, <scene name='pdbligand=OH:HYDROXIDE+ION'>OH</scene></td></tr>
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==Reference==
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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=2huo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2huo OCA], [https://pdbe.org/2huo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2huo RCSB], [https://www.ebi.ac.uk/pdbsum/2huo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2huo ProSAT]</span></td></tr>
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Crystal structure of a substrate complex of myo-inositol oxygenase, a di-iron oxygenase with a key role in inositol metabolism., Brown PM, Caradoc-Davies TT, Dickson JM, Cooper GJ, Loomes KM, Baker EN, Proc Natl Acad Sci U S A. 2006 Oct 10;103(41):15032-7. Epub 2006 Sep 29. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17012379 17012379]
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</table>
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[[Category: Inositol oxygenase]]
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== Function ==
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[https://www.uniprot.org/uniprot/MIOX_MOUSE MIOX_MOUSE]
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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/hu/2huo_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=2huo ConSurf].
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<div style="clear:both"></div>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
[[Category: Mus musculus]]
[[Category: Mus musculus]]
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[[Category: Single protein]]
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[[Category: Baker EN]]
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[[Category: Baker, E.N.]]
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[[Category: Brown PM]]
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[[Category: Brown, P.M.]]
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[[Category: Caradoc-Davies TT]]
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[[Category: Caradoc-Davies, T.T.]]
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[[Category: Cooper GJS]]
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[[Category: Cooper, G.J.S.]]
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[[Category: Dickson JMJ]]
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[[Category: Dickson, J.M.J.]]
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[[Category: Loomes KM]]
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[[Category: Loomes, K.M.]]
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[[Category: FE]]
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[[Category: FMT]]
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[[Category: INS]]
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[[Category: OH]]
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[[Category: hd domain fold]]
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[[Category: protein-substrate complex]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 11:59:45 2007''
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Current revision

Crystal structure of mouse myo-inositol oxygenase in complex with substrate

PDB ID 2huo

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