6sdm: Difference between revisions
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<StructureSection load='6sdm' size='340' side='right'caption='[[6sdm]], [[Resolution|resolution]] 2.85Å' scene=''> | <StructureSection load='6sdm' size='340' side='right'caption='[[6sdm]], [[Resolution|resolution]] 2.85Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[6sdm]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[6sdm]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermoanaerobacter_brockii Thermoanaerobacter brockii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6SDM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6SDM FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.85Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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=6sdm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6sdm OCA], [https://pdbe.org/6sdm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6sdm RCSB], [https://www.ebi.ac.uk/pdbsum/6sdm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6sdm ProSAT]</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=6sdm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6sdm OCA], [https://pdbe.org/6sdm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6sdm RCSB], [https://www.ebi.ac.uk/pdbsum/6sdm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6sdm ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/ADH_THEBR ADH_THEBR] Alcohol dehydrogenase with a preference for medium chain secondary alcohols, such as 2-butanol and isopropanol. Has very low activity with primary alcohols, such as ethanol. Under physiological conditions, the enzyme reduces aldehydes and 2-ketones to produce secondary alcohols. Is also active with acetaldehyde and propionaldehyde. | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: | [[Category: Thermoanaerobacter brockii]] | ||
[[Category: | [[Category: Heap JT]] | ||
[[Category: | [[Category: Murray JW]] | ||
[[Category: | [[Category: Selles Vidal L]] | ||
Latest revision as of 15:39, 24 January 2024
NADH-dependent variant of TBADHNADH-dependent variant of TBADH
Structural highlights
FunctionADH_THEBR Alcohol dehydrogenase with a preference for medium chain secondary alcohols, such as 2-butanol and isopropanol. Has very low activity with primary alcohols, such as ethanol. Under physiological conditions, the enzyme reduces aldehydes and 2-ketones to produce secondary alcohols. Is also active with acetaldehyde and propionaldehyde. Publication Abstract from PubMedThe non-natural needs of industrial applications often require new or improved enzymes. The structures and properties of enzymes are difficult to predict or design de novo. Instead, semi-rational approaches mimicking evolution entail diversification of parent enzymes followed by evaluation of isolated variants. Artificial selection pressures coupling desired enzyme properties to cell growth could overcome this key bottleneck, but are usually narrow in scope. Here we show diverse enzymes using the ubiquitous cofactors nicotinamide adenine dinucleotide (NAD) or nicotinamide adenine dinucleotide phosphate (NADP) can substitute for defective NAD regeneration, representing a very broadly-applicable artificial selection. Inactivation of Escherichia coli genes required for anaerobic NAD regeneration causes a conditional growth defect. Cells are rescued by foreign enzymes connected to the metabolic network only via NAD or NADP, but only when their substrates are supplied. Using this principle, alcohol dehydrogenase, imine reductase and nitroreductase variants with desired selectivity modifications, and a high-performing isopropanol metabolic pathway, are isolated from libraries of millions of variants in single-round experiments with typical limited information to guide design. Versatile selective evolutionary pressure using synthetic defect in universal metabolism.,Selles Vidal L, Murray JW, Heap JT Nat Commun. 2021 Nov 25;12(1):6859. doi: 10.1038/s41467-021-27266-9. PMID:34824282[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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