4pne

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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=4pne FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4pne OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4pne RCSB], [http://www.ebi.ac.uk/pdbsum/4pne 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=4pne FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4pne OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4pne RCSB], [http://www.ebi.ac.uk/pdbsum/4pne PDBsum]</span></td></tr>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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In the biosynthetic pathway of the spinosyn insecticides, the tailoring enzyme SpnF performs a [4 + 2] cycloaddition on a 22-membered macrolactone to forge an embedded cyclohexene ring. To learn more about this reaction, which could potentially proceed through a Diels-Alder mechanism, we determined the 1.50-A-resolution crystal structure of SpnF bound to S-adenosylhomocysteine. This sets the stage for advanced experimental and computational studies to determine the precise mechanism of SpnF-mediated cyclization.
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The structure of SpnF, a standalone enzyme that catalyzes [4 + 2] cycloaddition.,Fage CD, Isiorho EA, Liu Y, Wagner DT, Liu HW, Keatinge-Clay AT Nat Chem Biol. 2015 Mar 2. doi: 10.1038/nchembio.1768. PMID:25730549<ref>PMID:25730549</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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== References ==
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<references/>
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Revision as of 05:40, 11 March 2015

Crystal Structure of the [4+2]-Cyclase SpnF

4pne, resolution 1.50Å

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