4rzm: Difference between revisions
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==Crystal structure of the Lsd19-lasalocid A complex== | ==Crystal structure of the Lsd19-lasalocid A complex== | ||
<StructureSection load='4rzm' size='340' side='right' caption='[[4rzm]], [[Resolution|resolution]] 2.33Å' scene=''> | <StructureSection load='4rzm' size='340' side='right' caption='[[4rzm]], [[Resolution|resolution]] 2.33Å' scene=''> | ||
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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>, <scene name='pdbligand=FMT:FORMIC+ACID'>FMT</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=LSD:LASALOCID+A'>LSD</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr> | </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=FMT:FORMIC+ACID'>FMT</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=LSD:LASALOCID+A'>LSD</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3rga|3rga]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3rga|3rga]]</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=4rzm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4rzm OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4rzm RCSB], [http://www.ebi.ac.uk/pdbsum/4rzm PDBsum]</span></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=4rzm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4rzm OCA], [http://pdbe.org/4rzm PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4rzm RCSB], [http://www.ebi.ac.uk/pdbsum/4rzm PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4rzm ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 4rzm" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Epoxide hydrolase|Epoxide hydrolase]] | |||
== References == | == References == | ||
<references/> | <references/> |
Revision as of 10:55, 11 August 2016
Crystal structure of the Lsd19-lasalocid A complexCrystal structure of the Lsd19-lasalocid A complex
Structural highlights
Function[LSD19_STRLS] Epoxide hydrolase responsible for the double epoxide-opening cyclization of bisepoxyprelasalocid A to form lasalocid A, a polyether antibiotic. In vitro, accepts various substrate analogs differing in the left segment of lasalocid and epoxide stereochemistry to afford products with excellent regioselectivity.[1] [2] [3] [4] Publication Abstract from PubMedBiosynthesis of some polyether natural products involves a kinetically disfavored epoxide-opening cyclic ether formation, a reaction termed anti-Baldwin cyclization. One such example is the biosynthesis of lasalocid A, an ionophore antibiotic polyether. During lasalocid A biosynthesis, an epoxide hydrolase, Lsd19, converts the bisepoxy polyketide intermediate into the tetrahydrofuranyl-tetrahydropyran product. We report the crystal structure of Lsd19 in complex with lasalocid A. The structure unambiguously shows that the C-terminal domain of Lsd19 catalyzes the intriguing anti-Baldwin cyclization. We propose a general mechanism for epoxide selection by ionophore polyether epoxide hydrolases. Epoxide hydrolase-lasalocid a structure provides mechanistic insight into polyether natural product biosynthesis.,Wong FT, Hotta K, Chen X, Fang M, Watanabe K, Kim CY J Am Chem Soc. 2015 Jan 14;137(1):86-9. doi: 10.1021/ja511374k. Epub 2014 Dec 31. PMID:25535803[5] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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