4pa8: Difference between revisions

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-'''Unreleased structure'''
+==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]] 1.20&Aring;' 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.
-The entry 4pa8 is ON HOLD  until Paper Publication
+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>
-Authors: Beck, T., Garrabou Pi, X., Hilvert, D.
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
-Description: Crystal structure of a de novo retro-aldolase catalyzing asymmetric Michael additions, with a covalently bound product analog
+== References ==
-[[Category: Unreleased Structures]]
+<references/>
+__TOC__
+</StructureSection>
 [[Category: Beck, T]]
 [[Category: Hilvert, D]]
-[[Category: Garrabou Pi, X]]
+[[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]]