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| | ==Hedycaryol apo== | | ==Hedycaryol apo== |
| - | <StructureSection load='4mc0' size='340' side='right' caption='[[4mc0]], [[Resolution|resolution]] 2.70Å' scene=''> | + | <StructureSection load='4mc0' size='340' side='right'caption='[[4mc0]], [[Resolution|resolution]] 2.70Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4mc0]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Kitsk Kitsk]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4MC0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4MC0 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4mc0]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Kitasatospora_setae_KM-6054 Kitasatospora setae KM-6054]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4MC0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4MC0 FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1hm4|1hm4]], [[4mc3|4mc3]], [[4mc8|4mc8]]</td></tr> | + | </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> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">KSE_00200t, KSE_76540t ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=452652 KITSK])</td></tr>
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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=4mc0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4mc0 OCA], [http://pdbe.org/4mc0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4mc0 RCSB], [http://www.ebi.ac.uk/pdbsum/4mc0 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4mc0 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/HCS_KITSK HCS_KITSK] Catalyzes the conversion of (2E,6E)-farnesyl diphosphate (FPP) into (2Z,6E)-hedycaryol via a 1,11-cyclization.<ref>PMID:24399794</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Kitsk]] | + | [[Category: Kitasatospora setae KM-6054]] |
| - | [[Category: Baer, P]] | + | [[Category: Large Structures]] |
| - | [[Category: Cirton, C]] | + | [[Category: Baer P]] |
| - | [[Category: Dickschat, J]] | + | [[Category: Cirton C]] |
| - | [[Category: Groll, M]] | + | [[Category: Dickschat J]] |
| - | [[Category: Kaufmann, N]] | + | [[Category: Groll M]] |
| - | [[Category: Mann, C Oliveira]] | + | [[Category: Kaufmann N]] |
| - | [[Category: Rabe, P]] | + | [[Category: Oliveira Mann C]] |
| - | [[Category: Cyclase]]
| + | [[Category: Rabe P]] |
| - | [[Category: Helix break]]
| + | |
| - | [[Category: Helix dipol]]
| + | |
| - | [[Category: Lyase]]
| + | |
| - | [[Category: Terpene alpha domain class i]]
| + | |
| - | [[Category: Terpenoid]]
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| Structural highlights
Function
HCS_KITSK Catalyzes the conversion of (2E,6E)-farnesyl diphosphate (FPP) into (2Z,6E)-hedycaryol via a 1,11-cyclization.[1]
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[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Baer P, Rabe P, Citron CA, de Oliveira Mann CC, Kaufmann N, Groll M, Dickschat JS. Hedycaryol synthase in complex with nerolidol reveals terpene cyclase mechanism. Chembiochem. 2014 Jan 24;15(2):213-6. doi: 10.1002/cbic.201300708. Epub 2014 Jan , 7. PMID:24399794 doi:http://dx.doi.org/10.1002/cbic.201300708
- ↑ Baer P, Rabe P, Citron CA, de Oliveira Mann CC, Kaufmann N, Groll M, Dickschat JS. Hedycaryol synthase in complex with nerolidol reveals terpene cyclase mechanism. Chembiochem. 2014 Jan 24;15(2):213-6. doi: 10.1002/cbic.201300708. Epub 2014 Jan , 7. PMID:24399794 doi:http://dx.doi.org/10.1002/cbic.201300708
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