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4pa8
From Proteopedia
(Difference between revisions)
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| - | ''' | + | ==Crystal structure of a de novo retro-aldolase catalyzing asymmetric Michael additions, with a covalently bound product analog== |
| + | <StructureSection load='4pa8' size='340' side='right' caption='[[4pa8]], [[Resolution|resolution]] 1.20Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[4pa8]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4PA8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4PA8 FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=2K6:(3R)-3-(4-METHOXYPHENYL)-5-OXOHEXANENITRILE'>2K6</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | ||
| + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4a29|4a29]], [[4a2s|4a2s]], [[4a2r|4a2r]]</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=4pa8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4pa8 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4pa8 RCSB], [http://www.ebi.ac.uk/pdbsum/4pa8 PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Recent advances in computational design have enabled the development of primitive enzymes for a range of mechanistically distinct reactions. Here we show that the rudimentary active sites of these catalysts can give rise to useful chemical promiscuity. Specifically, RA95.5-8, designed and evolved as a retro-aldolase, also promotes asymmetric Michael additions of carbanions to unsaturated ketones with high rates and selectivities. The reactions proceed by amine catalysis, as indicated by mutagenesis and X-ray data. The inherent flexibility and tunability of this catalyst should make it a versatile platform for further optimization and/or mechanistic diversification by directed evolution. | ||
| - | + | A Promiscuous De Novo Retro-Aldolase Catalyzes Asymmetric Michael Additions via Schiff Base Intermediates.,Garrabou X, Beck T, Hilvert D Angew Chem Int Ed Engl. 2015 Mar 16. doi: 10.1002/anie.201500217. PMID:25777153<ref>PMID:25777153</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | == References == | |
| - | + | <references/> | |
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Beck, T]] | [[Category: Beck, T]] | ||
[[Category: Hilvert, D]] | [[Category: Hilvert, D]] | ||
| - | [[Category: | + | [[Category: Pi, X Garrabou]] |
| + | [[Category: Aldolase]] | ||
| + | [[Category: Artificial catalyst]] | ||
| + | [[Category: Computer-aided design]] | ||
| + | [[Category: De novo protein]] | ||
| + | [[Category: Directed evolution]] | ||
| + | [[Category: Enzyme design]] | ||
| + | [[Category: Enzyme-product analog complex]] | ||
| + | [[Category: Hydrolase]] | ||
| + | [[Category: Michael addition]] | ||
| + | [[Category: Protein engineering]] | ||
| + | [[Category: Retro-aldolase]] | ||
| + | [[Category: Substrate specificity]] | ||
| + | [[Category: Tim-barrel fold]] | ||
Revision as of 13:15, 1 April 2015
Crystal structure of a de novo retro-aldolase catalyzing asymmetric Michael additions, with a covalently bound product analog
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Categories: Beck, T | Hilvert, D | Pi, X Garrabou | Aldolase | Artificial catalyst | Computer-aided design | De novo protein | Directed evolution | Enzyme design | Enzyme-product analog complex | Hydrolase | Michael addition | Protein engineering | Retro-aldolase | Substrate specificity | Tim-barrel fold
