1h2b

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[[Image:1h2b.gif|left|200px]]<br />
 
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<applet load="1h2b" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1h2b, resolution 1.62&Aring;" />
 
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'''CRYSTAL STRUCTURE OF THE ALCOHOL DEHYDROGENASE FROM THE HYPERTHERMOPHILIC ARCHAEON AEROPYRUM PERNIX AT 1.65A RESOLUTION'''<br />
 
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==Overview==
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==Crystal Structure of the Alcohol Dehydrogenase from the Hyperthermophilic Archaeon Aeropyrum pernix at 1.65A Resolution==
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The structure of the recombinant medium chain alcohol dehydrogenase (ADH), from the hyperthermophilic archaeon Aeropyrum pernix has been solved by, the multiple anomalous dispersion technique using the signal from the, naturally occurring zinc ions. The enzyme is a tetramer with 222 point, group symmetry. The ADH monomer is formed from a catalytic and a, cofactor-binding domain, with the overall fold similar to previously, solved ADH structures. The 1.62 A resolution A.pernix ADH structure is, that of the holo form, with the cofactor NADH bound into the cleft between, the two domains. The electron density found in the active site has been, interpreted to be octanoic acid, which has been shown to be an inhibitor, of the enzyme. This inhibitor is positioned with its carbonyl oxygen atom, forming the fourth ligand of the catalytic zinc ion. The structural zinc, ion of each monomer is present at only partial occupancy and in its, absence a disulfide bond is formed. The enhanced thermal stability of the, A.pernix ADH is thought to arise primarily from increased ionic and, hydrophobic interactions on the subunit interfaces.
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<StructureSection load='1h2b' size='340' side='right'caption='[[1h2b]], [[Resolution|resolution]] 1.62&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1h2b]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Aeropyrum_pernix Aeropyrum pernix]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1H2B OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1H2B 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]] 1.62&#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=NAJ:NICOTINAMIDE-ADENINE-DINUCLEOTIDE+(ACIDIC+FORM)'>NAJ</scene>, <scene name='pdbligand=OCA:OCTANOIC+ACID+(CAPRYLIC+ACID)'>OCA</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=1h2b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1h2b OCA], [https://pdbe.org/1h2b PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1h2b RCSB], [https://www.ebi.ac.uk/pdbsum/1h2b PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1h2b ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/Q9Y9P9_AERPE Q9Y9P9_AERPE]
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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/h2/1h2b_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=1h2b ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The structure of the recombinant medium chain alcohol dehydrogenase (ADH) from the hyperthermophilic archaeon Aeropyrum pernix has been solved by the multiple anomalous dispersion technique using the signal from the naturally occurring zinc ions. The enzyme is a tetramer with 222 point group symmetry. The ADH monomer is formed from a catalytic and a cofactor-binding domain, with the overall fold similar to previously solved ADH structures. The 1.62 A resolution A.pernix ADH structure is that of the holo form, with the cofactor NADH bound into the cleft between the two domains. The electron density found in the active site has been interpreted to be octanoic acid, which has been shown to be an inhibitor of the enzyme. This inhibitor is positioned with its carbonyl oxygen atom forming the fourth ligand of the catalytic zinc ion. The structural zinc ion of each monomer is present at only partial occupancy and in its absence a disulfide bond is formed. The enhanced thermal stability of the A.pernix ADH is thought to arise primarily from increased ionic and hydrophobic interactions on the subunit interfaces.
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==About this Structure==
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The structure of an alcohol dehydrogenase from the hyperthermophilic archaeon Aeropyrum pernix.,Guy JE, Isupov MN, Littlechild JA J Mol Biol. 2003 Aug 29;331(5):1041-51. PMID:12927540<ref>PMID:12927540</ref>
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1H2B is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Aeropyrum_pernix Aeropyrum pernix] with ZN, OCA and NAJ as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Alcohol_dehydrogenase Alcohol dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.1 1.1.1.1] Structure known Active Site: OC1. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1H2B OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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The structure of an alcohol dehydrogenase from the hyperthermophilic archaeon Aeropyrum pernix., Guy JE, Isupov MN, Littlechild JA, J Mol Biol. 2003 Aug 29;331(5):1041-51. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12927540 12927540]
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</div>
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[[Category: Aeropyrum pernix]]
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<div class="pdbe-citations 1h2b" style="background-color:#fffaf0;"></div>
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[[Category: Alcohol dehydrogenase]]
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[[Category: Single protein]]
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[[Category: Guy, J.E.]]
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[[Category: Isupov, M.N.]]
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[[Category: Littlechild, J.A.]]
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[[Category: NAJ]]
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[[Category: OCA]]
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[[Category: ZN]]
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[[Category: alcohol dehydrogenase oxidoreductase]]
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[[Category: archaea]]
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[[Category: hyperthermophile]]
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[[Category: zinc]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 5 16:26:27 2007''
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==See Also==
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*[[Alcohol dehydrogenase 3D structures|Alcohol dehydrogenase 3D structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Aeropyrum pernix]]
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[[Category: Large Structures]]
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[[Category: Guy JE]]
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[[Category: Isupov MN]]
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[[Category: Littlechild JA]]

Current revision

Crystal Structure of the Alcohol Dehydrogenase from the Hyperthermophilic Archaeon Aeropyrum pernix at 1.65A Resolution

PDB ID 1h2b

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