4mc0

</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=4mc0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4mc0 OCA], [https://pdbe.org/4mc0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4mc0 RCSB], [https://www.ebi.ac.uk/pdbsum/4mc0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4mc0 ProSAT]</span></td></tr>

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== Publication Abstract from PubMed ==

The biosynthesis of terpenes is catalysed by class I and II terpene cyclases. Here we present structural data from a class I hedycaryol synthase in complex with nerolidol, serving as a surrogate for the reaction intermediate nerolidyl diphosphate. This prefolded ligand allows mapping of the active site and hence the identification of a key carbonyl oxygen of Val179, a highly conserved helix break (G1/2) and its corresponding helix dipole. Stabilising the carbocation at the substrate's C1 position, these elements act in concert to catalyse the 1,10 ring closure, thereby exclusively generating the anti-Markovnikov product. The delineation of a general mechanistic scaffold was confirmed by site-specific mutations. This work serves as a basis for understanding carbocation chemistry in enzymatic reactions and should contribute to future application of these enzymes in organic synthesis.

Hedycaryol synthase in complex with nerolidol reveals terpene cyclase mechanism.,Baer P, Rabe P, Citron CA, de Oliveira Mann CC, Kaufmann N, Groll M, Dickschat JS Chembiochem. 2014 Jan 24;15(2):213-6. doi: 10.1002/cbic.201300708. Epub 2014 Jan , 7. PMID:24399794<ref>PMID:24399794</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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