1teh

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[[Image:1teh.jpg|left|200px]]<br /><applet load="1teh" size="350" color="white" frame="true" align="right" spinBox="true"
 
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caption="1teh, resolution 2.7&Aring;" />
 
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'''STRUCTURE OF HUMAN LIVER CHICHI ALCOHOL DEHYDROGENASE (A GLUTATHIONE-DEPENDENT FORMALDEHYDE DEHYDROGENASE)'''<br />
 
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==Overview==
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==STRUCTURE OF HUMAN LIVER CHICHI ALCOHOL DEHYDROGENASE (A GLUTATHIONE-DEPENDENT FORMALDEHYDE DEHYDROGENASE)==
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The crystal structure of the human class III chi chi alcohol dehydrogenase, (ADH) in a binary complex with NAD+(gamma) was solved to 2.7 A resolution, by molecular replacement with human class I beta1 beta1 ADH. chi chi ADH, catalyzes the oxidation of long-chain alcohols such as omega-hydroxy fatty, acids as well as S-hydroxymethyl-glutathione, a spontaneous adduct between, formaldehyde and glutathione. There are two subunits per asymmetric unit, in the chi chi ADH structure. Both subunits display a semi-open, conformation of the catalytic domain. This conformation is half-way, between the open and closed conformations described for the horse EE ADH, enzyme. The semi-open conformation and key changes in elements of, secondary structure provide a structural basis for the ability of chi chi, ADH to bind S-hydroxymethyl-glutathione and 10-hydroxydecanoate. Direct, coordination of the catalytic zinc ion by Glu68 creates a novel, environment for the catalytic zinc ion in chi chi ADH. This new, configuration of the catalytic zinc is similar to an intermediate for, horse EE ADH proposed through theoretical computations and is consistent, with the spectroscopic data of the Co(II)-substituted chi chi enzyme. The, position for residue His47 in the chi chi ADH structure suggests His47 may, function both as a catalytic base for proton transfer and in the binding, of the adenosine phosphate of NAD(H). Modeling of substrate binding to, this enzyme structure is consistent with prior mutagenesis data which, showed that both Asp57 and Arg115 contribute to glutathione binding and, that Arg115 contributes to the binding of omega-hydroxy fatty acids and, identifies additional residues which may contribute to substrate binding.
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<StructureSection load='1teh' size='340' side='right'caption='[[1teh]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1teh]] 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=1TEH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1TEH 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]] 2.7&#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=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=1teh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1teh OCA], [https://pdbe.org/1teh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1teh RCSB], [https://www.ebi.ac.uk/pdbsum/1teh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1teh ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/ADHX_HUMAN ADHX_HUMAN] Class-III ADH is remarkably ineffective in oxidizing ethanol, but it readily catalyzes the oxidation of long-chain primary alcohols and the oxidation of S-(hydroxymethyl) glutathione.
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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/te/1teh_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=1teh 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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1TEH 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=ZN:'>ZN</scene> and <scene name='pdbligand=NAD:'>NAD</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Known structural/functional Sites: <scene name='pdbsite=ZN1:Zna1+In+Chitoph19.Znc+And+Chiparam1.Znc'>ZN1</scene>, <scene name='pdbsite=ZN2:GLU+68+Is+Nearly-Coordinated+To+The+Zn,+2.87+Angstroms.+...'>ZN2</scene>, <scene name='pdbsite=ZN3:Znb1+In+Chitoph19.Znc+And+Chiparam1.Znc'>ZN3</scene>, <scene name='pdbsite=ZN4:GLU+68+Is+Coordinated+To+The+Zn,+2.04+Angstroms.+Znb+In+...'>ZN4</scene> and <scene name='pdbsite=ZNS:This+Zn+Is+Positioned+On+Crystallographic+X+Axis,+Theref+...'>ZNS</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TEH OCA].
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*[[Alcohol dehydrogenase 3D structures|Alcohol dehydrogenase 3D structures]]
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__TOC__
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==Reference==
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</StructureSection>
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Structure of human chi chi alcohol dehydrogenase: a glutathione-dependent formaldehyde dehydrogenase., Yang ZN, Bosron WF, Hurley TD, J Mol Biol. 1997 Jan 24;265(3):330-43. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9018047 9018047]
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Hurley, T.D.]]
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[[Category: Hurley TD]]
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[[Category: Yang, Z.N.]]
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[[Category: Yang Z-N]]
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[[Category: NAD]]
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[[Category: ZN]]
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[[Category: nad+ dependent alcohol dehydrogenase glutathione dependent formaldehyde dehydrogenase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 10:02:24 2008''
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Current revision

STRUCTURE OF HUMAN LIVER CHICHI ALCOHOL DEHYDROGENASE (A GLUTATHIONE-DEPENDENT FORMALDEHYDE DEHYDROGENASE)

PDB ID 1teh

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