4pa8: Difference between revisions
New page: '''Unreleased structure''' The entry 4pa8 is ON HOLD Authors: Beck,T., Garrabou Pi, X., Hilvert,D. Description: Crystal structure of a de novo retro-aldolase catalyzing asymmetric Mich... |
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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 with sequence from [https://en.wikipedia.org/wiki/Saccharolobus_solfataricus Saccharolobus solfataricus]. 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 [https://proteopedia.org/fgij/fg.htm?mol=4PA8 FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.2Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4pa8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4pa8 OCA], [https://pdbe.org/4pa8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4pa8 RCSB], [https://www.ebi.ac.uk/pdbsum/4pa8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4pa8 ProSAT]</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> | |||
<div class="pdbe-citations 4pa8" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Aldolase 3D structures|Aldolase 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Saccharolobus solfataricus]] | |||
[[Category: Beck T]] | |||
[[Category: Garrabou Pi X]] | |||
[[Category: Hilvert D]] | |||