8xyn: Difference between revisions

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'''Unreleased structure'''


The entry 8xyn is ON HOLD  until Paper Publication
==Structure of the engineered retro-aldolase RA95.5-8==
<StructureSection load='8xyn' size='340' side='right'caption='[[8xyn]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[8xyn]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8XYN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8XYN 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]] 2.3&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=A1LXX:4-[dodecyl(dimethyl)-$l^{4}-azanyl]butanoic+acid'>A1LXX</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=8xyn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8xyn OCA], [https://pdbe.org/8xyn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8xyn RCSB], [https://www.ebi.ac.uk/pdbsum/8xyn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8xyn ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The introduction of an abiological catalytic group into the binding pocket of a protein host allows for the expansion of enzyme chemistries. Here, we report the generation of an artificial enzyme by genetic encoding of a non-canonical amino acid that contains a secondary amine side chain. The non-canonical amino acid and the binding pocket function synergistically to catalyze the asymmetric nitrocyclopropanation of alpha,beta-unsaturated aldehydes by the iminium activation mechanism. The designer enzyme was evolved to an optimal variant that catalyzes the reaction at high conversions with high diastereo- and enantioselectivity. This work demonstrates the application of genetic code expansion in enzyme design and expands the scope of enzyme-catalyzed abiological reactions.


Authors: Kunthic, T., Yu, M.Z., Xiang, Z.
An Artificial Enzyme for Asymmetric Nitrocyclopropanation of alpha,beta-Unsaturated Aldehydes-Design and Evolution.,Yu MZ, Yuan Y, Li ZJ, Kunthic T, Wang HX, Xu C, Xiang Z Angew Chem Int Ed Engl. 2024 Jun 17;63(25):e202401635. doi: , 10.1002/anie.202401635. Epub 2024 May 14. PMID:38597773<ref>PMID:38597773</ref>


Description: Structure of the engineered retro-aldolase RA95.5-8
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
[[Category: Kunthic, T]]
<div class="pdbe-citations 8xyn" style="background-color:#fffaf0;"></div>
[[Category: Yu, M.Z]]
== References ==
[[Category: Xiang, Z]]
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Synthetic construct]]
[[Category: Kunthic T]]
[[Category: Xiang Z]]
[[Category: Yu MZ]]
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