View source for 8qdh


==Engineered LmrR carrying a cyclic boronate ester formed between Tris and p-boronophenylalanine at position 89==
<StructureSection load='8qdh' size='340' side='right'caption='[[8qdh]], [[Resolution|resolution]] 1.72&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[8qdh]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Lactococcus_lactis_subsp._cremoris_MG1363 Lactococcus lactis subsp. cremoris MG1363]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8QDH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8QDH 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]] 1.72&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SD0:(S)-5-amino-2-(4-(2-amino-2-carboxyethyl)phenyl)-2-hydroxy-5-(hydroxymethyl)-1,3,2-dioxaborinan-2-uide'>SD0</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=8qdh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8qdh OCA], [https://pdbe.org/8qdh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8qdh RCSB], [https://www.ebi.ac.uk/pdbsum/8qdh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8qdh ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A2RI36_LACLM A2RI36_LACLM] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Enzymes play an increasingly important role in improving the benignity and efficiency of chemical production, yet the diversity of their applications lags heavily behind chemical catalysts as a result of the relatively narrow range of reaction mechanisms of enzymes. The creation of enzymes containing non-biological functionalities facilitates reaction mechanisms outside nature's canon and paves the way towards fully programmable biocatalysis(1-3). Here we present a completely genetically encoded boronic-acid-containing designer enzyme with organocatalytic reactivity not achievable with natural or engineered biocatalysts(4,5). This boron enzyme catalyses the kinetic resolution of hydroxyketones by oxime formation, in which crucial interactions with the protein scaffold assist in the catalysis. A directed evolution campaign led to a variant with natural-enzyme-like enantioselectivities for several different substrates. The unique activation mode of the boron enzyme was confirmed using X-ray crystallography, high-resolution mass spectrometry (HRMS) and (11)B NMR spectroscopy. Our study demonstrates that genetic-code expansion can be used to create evolvable enantioselective enzymes that rely on xenobiotic catalytic moieties such as boronic acids and access reaction mechanisms not reachable through catalytic promiscuity of natural or engineered enzymes.

Boron catalysis in a designer enzyme.,Longwitz L, Leveson-Gower RB, Rozeboom HJ, Thunnissen AWH, Roelfes G Nature. 2024 May;629(8013):824-829. doi: 10.1038/s41586-024-07391-3. Epub 2024 , May 8. PMID:38720081<ref>PMID:38720081</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 8qdh" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Lactococcus lactis subsp. cremoris MG1363]]
[[Category: Large Structures]]
[[Category: Leveson-Gower RB]]
[[Category: Longwitz L]]
[[Category: Roelfes G]]
[[Category: Rozeboom HJ]]
[[Category: Thunnissen AMWH]]