6tfa: Difference between revisions
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<StructureSection load='6tfa' size='340' side='right'caption='[[6tfa]], [[Resolution|resolution]] 2.16Å' scene=''> | <StructureSection load='6tfa' size='340' side='right'caption='[[6tfa]], [[Resolution|resolution]] 2.16Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[6tfa]] is a 4 chain structure with sequence from [ | <table><tr><td colspan='2'>[[6tfa]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Sacs2 Sacs2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6TFA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6TFA FirstGlance]. <br> | ||
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | </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=6tfa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6tfa OCA], [https://pdbe.org/6tfa PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6tfa RCSB], [https://www.ebi.ac.uk/pdbsum/6tfa PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6tfa ProSAT]</span></td></tr> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
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</div> | </div> | ||
<div class="pdbe-citations 6tfa" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 6tfa" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Aldolase 3D structures|Aldolase 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 18:18, 8 June 2021
Structure of the engineered retro-aldolase RA95.5-8F F112LStructure of the engineered retro-aldolase RA95.5-8F F112L
Structural highlights
Publication Abstract from PubMedControlling regio- and stereoselectivity of aldol additions is generally challenging. Here we show that an artificial aldolase with high specificity for acetone as the aldol donor can be reengineered via single active site mutations to accept linear and cyclic aliphatic ketones with notable efficiency, regioselectivity, and stereocontrol. Biochemical and crystallographic data show how the mutated residues modulate the binding and activation of specific aldol donors, as well as their subsequent reaction with diverse aldehyde acceptors. Broadening the substrate scope of this evolutionarily naive catalyst proved much easier than previous attempts to redesign natural aldolases, suggesting that such proteins may be excellent starting points for the development of customized biocatalysts for diverse practical applications. Engineered Artificial Carboligases Facilitate Regioselective Preparation of Enantioenriched Aldol Adducts.,Macdonald DS, Garrabou X, Klaus C, Verez R, Mori T, Hilvert D J Am Chem Soc. 2020 Jun 10;142(23):10250-10254. doi: 10.1021/jacs.0c02351. Epub, 2020 May 28. PMID:32427470[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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