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5b12

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==Crystal structure of the B-type halohydrin hydrogen-halide-lyase mutant F71W/Q125T/D199H from Corynebacterium sp. N-1074==
==Crystal structure of the B-type halohydrin hydrogen-halide-lyase mutant F71W/Q125T/D199H from Corynebacterium sp. N-1074==
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<StructureSection load='5b12' size='340' side='right' caption='[[5b12]], [[Resolution|resolution]] 1.72&Aring;' scene=''>
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<StructureSection load='5b12' size='340' side='right'caption='[[5b12]], [[Resolution|resolution]] 1.72&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5b12]] is a 6 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5B12 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5B12 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5b12]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Corynebacterium_sp. Corynebacterium sp.]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5B12 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5B12 FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.721&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5b12 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5b12 OCA], [http://pdbe.org/5b12 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5b12 RCSB], [http://www.ebi.ac.uk/pdbsum/5b12 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5b12 ProSAT]</span></td></tr>
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<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>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5b12 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5b12 OCA], [https://pdbe.org/5b12 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5b12 RCSB], [https://www.ebi.ac.uk/pdbsum/5b12 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5b12 ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/Q46347_CORSP Q46347_CORSP]
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Halohydrin hydrogen-halide-lyase (H-Lyase) is a bacterial enzyme involved in the degradation of halohydrins. This enzyme catalyzes the intramolecular nucleophilic displacement of a halogen by a vicinal hydroxyl group in halohydrins, producing the corresponding epoxides. The H-Lyases have been classified into A, B and C subtypes based on amino acid sequence similarities. These enzymes have attracted much attention as industrial catalysts in the synthesis of chiral chemicals from prochiral halohydrins. In the present study, we constructed mutants of B-type H-Lyase from Corynebacterium sp. N-1074 (HheB) displaying higher enantioselectivity by structure-based site-directed mutagenesis and random mutagenesis. A triple mutant of HheB exhibited 98.5% enantioselectivity, the highest ever reported, toward (R)-4-chloro-3-hydroxy-butyronitrile production, with the yield reaching approximately two-fold that of the wild-type enzyme. We discuss the structural basis of the high enantioselectivity and productivity of the mutant by comparing the crystal structures of the mutant HheB and the wild-type enzyme in complex with or without the substrate analogue.
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Improvement of enantioselectivity of the B-type halohydrin hydrogen-halide-lyase from Corynebacterium sp. N-1074.,Watanabe F, Yu F, Ohtaki A, Yamanaka Y, Noguchi K, Odaka M, Yohda M J Biosci Bioeng. 2016 Sep;122(3):270-5. doi: 10.1016/j.jbiosc.2016.02.003. Epub, 2016 May 20. PMID:27215832<ref>PMID:27215832</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 5b12" style="background-color:#fffaf0;"></div>
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==See Also==
==See Also==
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*[[Epoxidase|Epoxidase]]
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*[[Epoxidase 3D structures|Epoxidase 3D structures]]
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Noguchi, K]]
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[[Category: Corynebacterium sp]]
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[[Category: Odaka, M]]
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[[Category: Large Structures]]
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[[Category: Ohtaki, A]]
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[[Category: Noguchi K]]
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[[Category: Watanabe, F]]
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[[Category: Odaka M]]
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[[Category: Yamanaka, Y]]
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[[Category: Ohtaki A]]
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[[Category: Yohda, M]]
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[[Category: Watanabe F]]
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[[Category: Yu, F]]
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[[Category: Yamanaka Y]]
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[[Category: Enantioselectivity]]
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[[Category: Yohda M]]
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[[Category: Halohydrin]]
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[[Category: Yu F]]
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[[Category: Lyase]]
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Current revision

Crystal structure of the B-type halohydrin hydrogen-halide-lyase mutant F71W/Q125T/D199H from Corynebacterium sp. N-1074

PDB ID 5b12

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