1mp0

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[[Image:1mp0.jpg|left|200px]]<br /><applet load="1mp0" size="350" color="white" frame="true" align="right" spinBox="true"
 
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caption="1mp0, resolution 2.20&Aring;" />
 
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'''Binary Complex of Human Glutathione-Dependent Formaldehyde Dehydrogenase with NAD(H)'''<br />
 
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==Overview==
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==Binary Complex of Human Glutathione-Dependent Formaldehyde Dehydrogenase with NAD(H)==
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Human Class III alcohol dehydrogenase (ADH), also known as, glutathione-dependent formaldehyde dehydrogenase plays an important role, in the formaldehyde detoxification and reduction of the nitric oxide, metabolite s-nitrosoglutathione (GSNO). It follows a random bi bi kinetic, mechanism and prefers bulkier substrates like long chain primary alcohols, and glutathione adducts like s-hydroxymethylglutathione and GSNO over, smaller alcohols like ethanol. The structure of the FDH.NAD(H) binary, complex reported here, in conjunction with the other complexes of FDH, provide the structural basis of the kinetic observations. These structures, show that the apoenzyme has a semi-open domain conformation that permits, random random addition of alcohol or NAD(H). Moreover, there is no, significant domain movement upon binding of the coenzyme or the substrate, 12-hydroxydodecanoic acid. Interestingly, two active site zinc, coordination environments are observed in FDH. In the apoenzyme, the, active site zinc is coordinated to Cys44, His66, Cys173 and a water, molecule. In the FDH.NAD(H) binary complex reported here, Glu67 is added, to the coordination environment of the active site zinc and the distance, between the water molecule and zinc is increased. This change in the zinc, coordination, brought about by the displacement of zinc of about 2 A, towards Glu67 could promote substrate exchange at the active site metal, during catalysis.
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<StructureSection load='1mp0' size='340' side='right'caption='[[1mp0]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1mp0]] 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=1MP0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MP0 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]] 2.2&#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=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</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=1mp0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mp0 OCA], [https://pdbe.org/1mp0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1mp0 RCSB], [https://www.ebi.ac.uk/pdbsum/1mp0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1mp0 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/mp/1mp0_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=1mp0 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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1MP0 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>, <scene name='pdbligand=K:'>K</scene>, <scene name='pdbligand=PO4:'>PO4</scene> and <scene name='pdbligand=NAD:'>NAD</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MP0 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-function relationships in human Class III alcohol dehydrogenase (formaldehyde dehydrogenase)., Sanghani PC, Robinson H, Bennett-Lovsey R, Hurley TD, Bosron WF, Chem Biol Interact. 2003 Feb 1;143-144:195-200. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12604204 12604204]
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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: Bosron, W.F.]]
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[[Category: Bosron WF]]
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[[Category: Hurley, T.D.]]
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[[Category: Hurley TD]]
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[[Category: Robinson, H.]]
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[[Category: Robinson H]]
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[[Category: Sanghani, P.C.]]
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[[Category: Sanghani PC]]
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[[Category: K]]
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[[Category: NAD]]
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[[Category: PO4]]
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[[Category: ZN]]
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[[Category: class iii alcohol dehydrogenase]]
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[[Category: glutathione dependent formaldehyde dehydrogenase]]
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[[Category: mad]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 16:25:01 2008''
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Current revision

Binary Complex of Human Glutathione-Dependent Formaldehyde Dehydrogenase with NAD(H)

PDB ID 1mp0

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