View source for 4ufp


==Laboratory evolved variant R-C1B1D33 of potato epoxide hydrolase StEH1==
<StructureSection load='4ufp' size='340' side='right'caption='[[4ufp]], [[Resolution|resolution]] 2.95&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4ufp]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Solanum_tuberosum Solanum tuberosum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4UFP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4UFP 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]] 2.95&#8491;</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=4ufp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ufp OCA], [https://pdbe.org/4ufp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ufp RCSB], [https://www.ebi.ac.uk/pdbsum/4ufp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ufp ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q41415_SOLTU Q41415_SOLTU] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Engineered enzyme variants of potato epoxide hydrolase (StEH1) display varying degrees of enrichment of (2R)-3-phenylpropane-1,2-diol from racemic benzyloxirane. Curiously, the observed increase in the enantiomeric excess of the (R)-diol is not only due to changes in enantioselectivity for the preferred epoxide enantiomer, but also to changes in the regioselectivity of the epoxide ring opening of (S)-benzyloxirane. To probe the structural origin of these differences in substrate selectivities and catalytic regiopreferences, we have solved the crystal structures for the in-vitro evolved StEH1 variants. We have additionally used these structures as a starting point for docking the epoxide enantiomers into the respective active sites. Interestingly, despite the simplicity of our docking calculations, the apparent preferred binding modes obtained from the docking appears to rationalize the experimentally determined regioselectivities. These calculations could also identify an active site residue (F33) as a putatively important interaction partner, a role that could explain the high degree of conservation of this residue during evolution. Overall, our combined experimental, structural and computational studies of this system provide snapshots into the evolution of enantioconvergence in StEH1 catalyzed epoxide hydrolysis.

Laboratory Evolved Enzymes Provide Snapshots of the Development of Enantioconvergence in Enzyme-Catalyzed Epoxide Hydrolysis.,Janfalk Carlsson A, Bauer P, Dobritzsch D, Nilsson M, Kamerlin SC, Widersten M Chembiochem. 2016 Jul 7. doi: 10.1002/cbic.201600330. PMID:27383542<ref>PMID:27383542</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4ufp" style="background-color:#fffaf0;"></div>

==See Also==
*[[Epoxide hydrolase 3D structures|Epoxide hydrolase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Solanum tuberosum]]
[[Category: Bauer P]]
[[Category: Carlsson AJ]]
[[Category: Dobritzsch D]]
[[Category: Kamerlin SCL]]
[[Category: Nilsson M]]
[[Category: Widersten M]]