View source for 8xxb


==Crystal Structure of a triple-mutant (A69F/M124P/R127G) of halohydrin dehalogenase HheD8 complexed with chloride==
<StructureSection load='8xxb' size='340' side='right'caption='[[8xxb]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[8xxb]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Thauera_aminoaromatica_S2 Thauera aminoaromatica S2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8XXB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8XXB 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]] 2.4&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</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=8xxb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8xxb OCA], [https://pdbe.org/8xxb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8xxb RCSB], [https://www.ebi.ac.uk/pdbsum/8xxb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8xxb ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/N6YXW4_THASP N6YXW4_THASP] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Although biocatalysis offers complementary or alternative approaches to traditional synthetic methods, the limited range of available enzymatic reactions currently poses challenges in synthesizing a diverse array of desired compounds. Consequently, there is a significant demand for developing novel biocatalytic processes to enable reactions that were previously unattainable. Herein, we report the discovery and subsequent protein engineering of a unique halohydrin dehalogenase to develop a biocatalytic platform for enantioselective formation and ring-opening of oxetanes. This biocatalytic platform, exhibiting high efficiency, excellent enantioselectivity, and broad scopes, facilitates the preparative-scale synthesis of chiral oxetanes and a variety of chiral gamma-substituted alcohols. Additionally, both the enantioselective oxetane formation and ring-opening processes are proven scalable for large-scale transformations at high substrate concentrations, and can be integrated efficiently in a one-pot, one-catalyst cascade system. This work expands the enzymatic toolbox for non-natural reactions and will promote further exploration of the catalytic repertoire of halohydrin dehalogenases in synthetic and pharmaceutical chemistry.

Biocatalytic enantioselective formation and ring-opening of oxetanes.,Hua X, Wang YF, Jin X, Yu HY, Wang HH, Chen YZ, Wan NW Nat Commun. 2025 Jan 30;16(1):1170. doi: 10.1038/s41467-025-56463-z. PMID:39885154<ref>PMID:39885154</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 8xxb" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Thauera aminoaromatica S2]]
[[Category: Wan NW]]