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| | ==YEAST ALCOHOL DEHYDROGENASE I, SACCHAROMYCES CEREVISIAE FERMENTATIVE ENZYME== | | ==YEAST ALCOHOL DEHYDROGENASE I, SACCHAROMYCES CEREVISIAE FERMENTATIVE ENZYME== |
| - | <StructureSection load='4w6z' size='340' side='right' caption='[[4w6z]], [[Resolution|resolution]] 2.40Å' scene=''> | + | <StructureSection load='4w6z' size='340' side='right'caption='[[4w6z]], [[Resolution|resolution]] 2.40Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4w6z]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Baker's_yeast Baker's yeast]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2hcy 2hcy]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4W6Z OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4W6Z FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4w6z]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2hcy 2hcy]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4W6Z OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4W6Z FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=8ID:NICOTINAMIDE-8-IODO-ADENINE-DINUCLEOTIDE'>8ID</scene>, <scene name='pdbligand=ETF:TRIFLUOROETHANOL'>ETF</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ADH1, ADC1, YOL086C, O0947 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=8ID:NICOTINAMIDE-8-IODO-ADENINE-DINUCLEOTIDE'>8ID</scene>, <scene name='pdbligand=ETF:TRIFLUOROETHANOL'>ETF</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </span></td></tr> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4w6z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4w6z OCA], [https://pdbe.org/4w6z PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4w6z RCSB], [https://www.ebi.ac.uk/pdbsum/4w6z PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4w6z ProSAT]</span></td></tr> |
| - | <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=4w6z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4w6z OCA], [http://pdbe.org/4w6z PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4w6z RCSB], [http://www.ebi.ac.uk/pdbsum/4w6z PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4w6z ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/ADH1_YEAST ADH1_YEAST]] This isozyme preferentially catalyzes the conversion of primary unbranched alcohols to their corresponding aldehydes. Also also shows activity toward secondary alcohols. | + | [https://www.uniprot.org/uniprot/ADH1_YEAST ADH1_YEAST] This isozyme preferentially catalyzes the conversion of primary unbranched alcohols to their corresponding aldehydes. Also also shows activity toward secondary alcohols. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </div> | | </div> |
| | <div class="pdbe-citations 4w6z" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 4w6z" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Alcohol dehydrogenase 3D structures|Alcohol dehydrogenase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Alcohol dehydrogenase]] | + | [[Category: Large Structures]] |
| - | [[Category: Baker's yeast]] | + | [[Category: Saccharomyces cerevisiae S288C]] |
| - | [[Category: Plapp, B v]] | + | [[Category: Plapp Bv]] |
| - | [[Category: Ramaswamy, s]] | + | [[Category: Ramaswamy s]] |
| - | [[Category: Savarimuthu, b r]] | + | [[Category: Savarimuthu br]] |
| - | [[Category: Intramolecular disulfide bond]]
| + | |
| - | [[Category: Oxidoreductase]]
| + | |
| - | [[Category: Tetramer of asymmetric dimer]]
| + | |
| - | [[Category: Zinc coordination]]
| + | |
| Structural highlights
Function
ADH1_YEAST This isozyme preferentially catalyzes the conversion of primary unbranched alcohols to their corresponding aldehydes. Also also shows activity toward secondary alcohols.
Publication Abstract from PubMed
Yeast (Saccharomyces cerevisiae) alcohol dehydrogenase I (ADH1) is the constitutive enzyme that reduces acetaldehyde to ethanol during fermentation of glucose. ADH1 is a homotetramer of subunits with 347 amino acid residues. A structure for ADH1 was determined by X-ray crystallography at 2.44 A resolution. The asymmetric unit contains four different subunits, arranged as similar dimers named AB and CD. The unit cell contains two different tetramers made up of "back-to-back" dimers, AB:AB and CD:CD. The A and C subunits in each dimer are structurally similar, with a closed conformation and bound coenzyme, and the 2,2,2-trifluoroethanol oxygen is ligated to the catalytic zinc in the classical tetrahedral coordination with Cys-43, Cys-153, and His-66. In contrast, the B and D subunits have an open conformation with no bound coenzyme, and the catalytic zinc has an alternative, inverted coordination with Cys-43, Cys-153, His-66 and the carboxylate of Glu-67. The asymmetry in the dimeric subunits of the tetramer provides two structures that appear to be relevant for the catalytic mechanism, even if there is no evidence of cooperativity in binding of coenzyme and kinetics. The alternative coordination of the zinc may represent an intermediate in the mechanism of displacement of the zinc-bound water with alcohol or aldehyde substrates. Substitution of Glu-67 with Gln-67 decreases catalytic efficiency by 100-fold. Previous studies on structural modeling, evolutionary relationships, substrate specificity, chemical modification and site-directed mutagenesis are interpreted more fully with the three-dimensional structure.
Yeast Alcohol Dehydrogenase Structure and Catalysis.,Raj SB, Ramaswamy S, Plapp BV Biochemistry. 2014 Aug 26. PMID:25157460[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Raj SB, Ramaswamy S, Plapp BV. Yeast Alcohol Dehydrogenase Structure and Catalysis. Biochemistry. 2014 Aug 26. PMID:25157460 doi:http://dx.doi.org/10.1021/bi5006442
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