1p0c

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(New page: 200px<br /><applet load="1p0c" size="450" color="white" frame="true" align="right" spinBox="true" caption="1p0c, resolution 2.2&Aring;" /> '''Crystal Structure of ...)
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[[Image:1p0c.jpg|left|200px]]<br /><applet load="1p0c" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1p0c, resolution 2.2&Aring;" />
 
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'''Crystal Structure of the NADP(H)-Dependent Vertebrate Alcohol Dehydrogenase (ADH8)'''<br />
 
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==Overview==
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==Crystal Structure of the NADP(H)-Dependent Vertebrate Alcohol Dehydrogenase (ADH8)==
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The amphibian enzyme ADH8, previously named class IV-like, is the only, known vertebrate alcohol dehydrogenase (ADH) with specificity towards, NADP(H). The three-dimensional structures of ADH8 and of the binary, complex ADH8-NADP(+) have been now determined and refined to resolutions, of 2.2A and 1.8A, respectively. The coenzyme and substrate specificity of, ADH8, that has 50-65% sequence identity with vertebrate NAD(H)-dependent, ADHs, suggest a role in aldehyde reduction probably as a retinal, reductase. The large volume of the substrate-binding pocket can explain, both the high catalytic efficiency of ADH8 with retinoids and the high, K(m) value for ethanol. Preference of NADP(H) appears to be achieved by, the presence in ADH8 of the triad Gly223-Thr224-His225 and the recruitment, of conserved Lys228, which define a binding pocket for the terminal, phosphate group of the cofactor. NADP(H) binds to ADH8 in an extended, conformation that superimposes well with the NAD(H) molecules found in, NAD(H)-dependent ADH complexes. No additional reshaping of the, dinucleotide-binding site is observed which explains why NAD(H) can also, be used as a cofactor by ADH8. The structural features support the, classification of ADH8 as an independent ADH class.
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<StructureSection load='1p0c' size='340' side='right'caption='[[1p0c]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1p0c]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Pelophylax_perezi Pelophylax perezi]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1P0C OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1P0C 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=GOL:GLYCEROL'>GOL</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=1p0c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1p0c OCA], [https://pdbe.org/1p0c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1p0c RCSB], [https://www.ebi.ac.uk/pdbsum/1p0c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1p0c ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/ADH8_PELPE ADH8_PELPE]
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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/p0/1p0c_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=1p0c 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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1P0C is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rana_porosa Rana porosa] with ZN, PO4 and GOL as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Alcohol_dehydrogenase_(NADP(+)) Alcohol dehydrogenase (NADP(+))], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.2 1.1.1.2] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1P0C 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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Crystal structure of the vertebrate NADP(H)-dependent alcohol dehydrogenase (ADH8)., Rosell A, Valencia E, Pares X, Fita I, Farres J, Ochoa WF, J Mol Biol. 2003 Jun 27;330(1):75-85. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12818203 12818203]
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[[Category: Large Structures]]
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[[Category: Alcohol dehydrogenase (NADP(+))]]
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[[Category: Pelophylax perezi]]
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[[Category: Rana porosa]]
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[[Category: Farres J]]
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[[Category: Single protein]]
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[[Category: Fita I]]
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[[Category: Farres, J.]]
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[[Category: Ochoa WF]]
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[[Category: Fita, I.]]
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[[Category: Pares X]]
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[[Category: Ochoa, W.F.]]
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[[Category: Rosell A]]
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[[Category: Pares, X.]]
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[[Category: Valencia E]]
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[[Category: Rosell, A.]]
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[[Category: Valencia, E.]]
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[[Category: GOL]]
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[[Category: PO4]]
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[[Category: ZN]]
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[[Category: adh topology]]
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[[Category: nadp(h)-dependent]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 23:20:33 2007''
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Current revision

Crystal Structure of the NADP(H)-Dependent Vertebrate Alcohol Dehydrogenase (ADH8)

PDB ID 1p0c

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