4pne: Difference between revisions
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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> | ||
</table> | </table> | ||
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== Publication Abstract from PubMed == | |||
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. | |||
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> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
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== References == | |||
<references/> | |||
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</StructureSection> | </StructureSection> | ||
