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6tf8
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Structure of the engineered artificial aldolase I133F RA95.5-8F with a bound substrate, pentan-2-one== | |
| + | <StructureSection load='6tf8' size='340' side='right'caption='[[6tf8]], [[Resolution|resolution]] 1.90Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[6tf8]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharolobus_solfataricus_P2 Saccharolobus solfataricus P2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6TF8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6TF8 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]] 1.903Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=N65:(2~{S})-2-azanyl-6-[(~{E})-pentan-2-ylideneamino]hexanal'>N65</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=6tf8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6tf8 OCA], [https://pdbe.org/6tf8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6tf8 RCSB], [https://www.ebi.ac.uk/pdbsum/6tf8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6tf8 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Controlling 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<ref>PMID:32427470</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 6tf8" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Saccharolobus solfataricus P2]] | ||
| + | [[Category: Macdonald DS]] | ||
| + | [[Category: Mori T]] | ||
Current revision
Structure of the engineered artificial aldolase I133F RA95.5-8F with a bound substrate, pentan-2-one
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