4xby: Difference between revisions
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<StructureSection load='4xby' size='340' side='right'caption='[[4xby]], [[Resolution|resolution]] 2.30Å' scene=''> | <StructureSection load='4xby' size='340' side='right'caption='[[4xby]], [[Resolution|resolution]] 2.30Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4xby]] is a 8 chain structure with sequence from [ | <table><tr><td colspan='2'>[[4xby]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Rhodococcus_erythropolis Rhodococcus erythropolis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4XBY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4XBY FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=3ZS:(1R,5S)-6-OXABICYCLO[3.1.0]HEXANE'>3ZS</scene | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=3ZS:(1R,5S)-6-OXABICYCLO[3.1.0]HEXANE'>3ZS</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=4xby FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4xby OCA], [https://pdbe.org/4xby PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4xby RCSB], [https://www.ebi.ac.uk/pdbsum/4xby PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4xby ProSAT]</span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/LIMA_RHOER LIMA_RHOER] Catalyzes the conversion of limonene-1,2-epoxide to limonene-1,2-diol. Can use both the (-) and (+) isomers of limonene-1,2-epoxide as substrates and also has some activity with 1-methylcyclohexene oxide, cyclohexene oxide and indene oxide as substrates. | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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==See Also== | ==See Also== | ||
*[[Epoxide hydrolase|Epoxide hydrolase]] | *[[Epoxide hydrolase 3D structures|Epoxide hydrolase 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: | [[Category: Rhodococcus erythropolis]] | ||
[[Category: Kong | [[Category: Kong XD]] | ||
[[Category: Reetz | [[Category: Reetz MT]] | ||
[[Category: Sun | [[Category: Sun Z]] | ||
[[Category: Xu | [[Category: Xu JH]] | ||
[[Category: Zhou | [[Category: Zhou J]] | ||
Revision as of 00:21, 13 April 2023
Crystal Structure of the L74F/M78V/I80V/L114F mutant of LEH complexed with cyclopentene oxideCrystal Structure of the L74F/M78V/I80V/L114F mutant of LEH complexed with cyclopentene oxide
Structural highlights
FunctionLIMA_RHOER Catalyzes the conversion of limonene-1,2-epoxide to limonene-1,2-diol. Can use both the (-) and (+) isomers of limonene-1,2-epoxide as substrates and also has some activity with 1-methylcyclohexene oxide, cyclohexene oxide and indene oxide as substrates. Publication Abstract from PubMedDirected evolution based on saturation mutagenesis at sites lining the binding pocket is a commonly practiced strategy for enhancing or inverting the stereoselectivity of enzymes for use in organic chemistry or biotechnology. However, as the number of residues in a randomization site increases to five or more, the screening effort for 95 % library coverage increases astronomically until it is no longer feasible. We propose the use of a single amino acid for saturation mutagenesis at superlarge randomization sites comprising 10 or more residues. When used to reshape the binding pocket of limonene epoxide hydrolase, this strategy, which drastically reduces the search space and thus the screening effort, resulted in R,R- and S,S-selective mutants for the hydrolytic desymmetrization of cyclohexene oxide and other epoxides. X-ray crystal structures and docking studies of the mutants unveiled the source of stereoselectivity and shed light on the mechanistic intricacies of this enzyme. Reshaping an Enzyme Binding Pocket for Enhanced and Inverted Stereoselectivity: Use of Smallest Amino Acid Alphabets in Directed Evolution.,Sun Z, Lonsdale R, Kong XD, Xu JH, Zhou J, Reetz MT Angew Chem Int Ed Engl. 2015 Apr 17. doi: 10.1002/anie.201501809. PMID:25891639[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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