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4fr2

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==Alcohol dehydrogenase from Oenococcus oeni==
==Alcohol dehydrogenase from Oenococcus oeni==
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<StructureSection load='4fr2' size='340' side='right' caption='[[4fr2]], [[Resolution|resolution]] 3.20&Aring;' scene=''>
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<StructureSection load='4fr2' size='340' side='right'caption='[[4fr2]], [[Resolution|resolution]] 3.20&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4fr2]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Oenococcus_oeni_atcc_baa-1163 Oenococcus oeni atcc baa-1163]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FR2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4FR2 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4fr2]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Oenococcus_oeni_ATCC_BAA-1163 Oenococcus oeni ATCC BAA-1163]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FR2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4FR2 FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene></td></tr>
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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]] 3.2&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">dhaT, OENOO_49030 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=379360 Oenococcus oeni ATCC BAA-1163])</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=NI:NICKEL+(II)+ION'>NI</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4fr2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fr2 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4fr2 RCSB], [http://www.ebi.ac.uk/pdbsum/4fr2 PDBsum]</span></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=4fr2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fr2 OCA], [https://pdbe.org/4fr2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4fr2 RCSB], [https://www.ebi.ac.uk/pdbsum/4fr2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4fr2 ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/A0NIJ1_OENOE A0NIJ1_OENOE]
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Alcohol dehydrogenases are highly diverse enzymes catalysing the interconversion of alcohols and aldehydes or ketones. Due to their versatile specificities, these biocatalysts are of great interest for industrial applications. The adh3-gene encoding a group III alcohol dehydrogenase was isolated from the gram-positive bacterium Oenococcus oeni and was characterised after expression in the heterologous host Escherichia coli. Adh3 has been identified by genome BLASTP analyses using the amino acid sequence of 1,3-propanediol dehydrogenase DhaT from Klebsiella pneumoniae and group III alcohol dehydrogenases with known activity towards 1,3-propanediol as target sequences. The recombinant protein was purified in a two-step column chromatography approach. Crystal structure determination and biochemical characterisation confirmed that Adh3 forms a Ni(2+)-containing homodimer in its active form. Adh3 catalyses the interconversion of ethanol and its corresponding aldehyde acetaldyhyde and is also capable of using other alcoholic compounds as substrates, such as 1,3-propanediol, 1,2-propanediol and 1-propanol. In the presence of Ni(2+), activity increases towards 1,3-propanediol and 1,2-propanediol. Adh3 is strictly dependent on NAD(+)/NADH, whereas no activity has been observed with NADP(+)/NADPH as co-factor. The enzyme exhibits a specific activity of 1.1 U/mg using EtOH as substrate with an optimal pH value of 9.0 for ethanol oxidation and 8.0 for aldehyde reduction. Moreover, Adh3 exhibits tolerance to several metal ions and organic solvents, but is completely inhibited in the presence of Zn(2+). The present study demonstrates that O. oeni is a group III alcohol dehydrogenase with versatile substrate specificity, including Ni(2+)-dependent activity towards 1,3-propanediol.
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Structural and biochemical characterisation of a NAD(+)-dependent alcohol dehydrogenase from Oenococcus oeni as a new model molecule for industrial biotechnology applications.,Elleuche S, Fodor K, Klippel B, von der Heyde A, Wilmanns M, Antranikian G Appl Microbiol Biotechnol. 2013 Feb 6. PMID:23385476<ref>PMID:23385476</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Oenococcus oeni atcc baa-1163]]
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[[Category: Large Structures]]
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[[Category: Fodor, K]]
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[[Category: Oenococcus oeni ATCC BAA-1163]]
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[[Category: Skander, E]]
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[[Category: Fodor K]]
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[[Category: Wilmanns, M]]
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[[Category: Skander E]]
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[[Category: Metal binding protein]]
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[[Category: Wilmanns M]]
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[[Category: Oxidoreductase]]
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[[Category: Rossmann fold]]
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Current revision

Alcohol dehydrogenase from Oenococcus oeni

PDB ID 4fr2

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