4zd6: Difference between revisions

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<StructureSection load='4zd6' size='340' side='right'caption='[[4zd6]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
<StructureSection load='4zd6' size='340' side='right'caption='[[4zd6]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4zd6]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Corsp Corsp]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ZD6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4ZD6 FirstGlance]. <br>
<table><tr><td colspan='2'>[[4zd6]] 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=4ZD6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4ZD6 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.6&#8491;</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">hheB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1720 CORSP])</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>, <scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
<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=4zd6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4zd6 OCA], [http://pdbe.org/4zd6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4zd6 RCSB], [http://www.ebi.ac.uk/pdbsum/4zd6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4zd6 ProSAT]</span></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=4zd6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4zd6 OCA], [https://pdbe.org/4zd6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4zd6 RCSB], [https://www.ebi.ac.uk/pdbsum/4zd6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4zd6 ProSAT]</span></td></tr>
</table>
</table>
<div style="background-color:#fffaf0;">
== Function ==
== Publication Abstract from PubMed ==
[https://www.uniprot.org/uniprot/Q46347_CORSP Q46347_CORSP]
Halohydrin hydrogen-halide-lyase (H-Lyase) is a bacterial enzyme that is involved in the degradation of halohydrins. This enzyme catalyzes the intramolecular nucleophilic displacement of a halogen by a vicinal hydroxyl group in halohydrins to produce the corresponding epoxides. The epoxide products are subsequently hydrolyzed by an epoxide hydrolase, yielding the corresponding 1, 2-diol. Until now, six different H-Lyases have been studied. These H-Lyases are grouped into three subtypes (A, B, and C) based on amino acid sequence similarities and exhibit different enantioselectivity. Corynebacterium sp. strain N-1074 has two different isozymes of H-Lyase, HheA (A-type) and HheB (B-type). We have determined their crystal structures to elucidate the differences in enantioselectivity among them. All three groups share a similar structure, including catalytic sites. The lack of enantioselectivity of HheA seems to be due to the relatively wide size of the substrate tunnel compared to that of other H-Lyases. Among the B-type H-Lyases, HheB shows relatively high enantioselectivity compared to that of HheBGP1 . This difference seems to be due to amino acid replacements at the active site tunnel. The binding mode of 1, 3-dicyano-2-propanol at the catalytic site in the crystal structure of the HheB-DiCN complex suggests that the product should be (R)-epichlorohydrin, which agrees with the enantioselectivity of HheB. Comparison with the structure of HheC provides a clue for the difference in their enantioselectivity. Proteins 2015; 83:2230-2239. (c) 2015 Wiley Periodicals, Inc.
 
Crystal structures of halohydrin hydrogen-halide-lyases from Corynebacterium sp. N-1074.,Watanabe F, Yu F, Ohtaki A, Yamanaka Y, Noguchi K, Yohda M, Odaka M Proteins. 2015 Dec;83(12):2230-9. doi: 10.1002/prot.24938. Epub 2015 Oct 16. PMID:26422370<ref>PMID:26422370</ref>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4zd6" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Epoxidase|Epoxidase]]
*[[Epoxidase 3D structures|Epoxidase 3D structures]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Corsp]]
[[Category: Corynebacterium sp]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Noguchi, K]]
[[Category: Noguchi K]]
[[Category: Odaka, M]]
[[Category: Odaka M]]
[[Category: Ohtaki, A]]
[[Category: Ohtaki A]]
[[Category: Watanabe, F]]
[[Category: Watanabe F]]
[[Category: Yamanaka, Y]]
[[Category: Yamanaka Y]]
[[Category: Yohda, M]]
[[Category: Yohda M]]
[[Category: Yu, F]]
[[Category: Yu F]]
[[Category: Lyase]]

Latest revision as of 09:04, 20 March 2024

Halohydrin hydrogen-halide-lyase, HheB

4zd6, resolution 1.60Å

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