5hc6: 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=5hc6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5hc6 OCA], [http://pdbe.org/5hc6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5hc6 RCSB], [http://www.ebi.ac.uk/pdbsum/5hc6 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=5hc6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5hc6 OCA], [http://pdbe.org/5hc6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5hc6 RCSB], [http://www.ebi.ac.uk/pdbsum/5hc6 PDBsum]</span></td></tr> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
We report the first X-ray structure of the unique "head-to-middle" monoterpene synthase, lavandulyl diphosphate synthase (LPPS). LPPS catalyzes the condensation of two molecules of dimethylallyl diphosphate (DMAPP) to form lavandulyl diphosphate, a precursor to the fragrance lavandulol. The structure is similar to that of the bacterial cis-prenyl synthase, undecaprenyl diphosphate synthase (UPPS), and contains an allylic site (S1) in which DMAPP ionizes and a second site (S2) which houses the DMAPP nucleophile. Both S-thiolo-dimethylallyl diphosphate and S-thiolo-isopentenyl diphosphate bind intact to S2, but are cleaved to (thio)diphosphate, in S1. His78 (Asn in UPPS) is essential for catalysis and is proposed to facilitate diphosphate release in S1, while the P1 phosphate in S2 abstracts a proton from the lavandulyl carbocation to form the LPP product. The results are of interest since they provide the first structure and structure-based mechanism of this unusual prenyl synthase. | |||
Structure and Function of a "Head-to-Middle" Prenyltransferase: Lavandulyl Diphosphate Synthase.,Liu M, Chen CC, Chen L, Xiao X, Zheng Y, Huang JW, Liu W, Ko TP, Cheng YS, Feng X, Oldfield E, Guo RT, Ma Y Angew Chem Int Ed Engl. 2016 Apr 4;55(15):4721-4. doi: 10.1002/anie.201600656., Epub 2016 Feb 29. PMID:26922900<ref>PMID:26922900</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
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<div class="pdbe-citations 5hc6" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Revision as of 19:50, 10 May 2016
Crystal structure of lavandulyl diphosphate synthase from Lavandula x intermedia in apo formCrystal structure of lavandulyl diphosphate synthase from Lavandula x intermedia in apo form
Structural highlights
Publication Abstract from PubMedWe report the first X-ray structure of the unique "head-to-middle" monoterpene synthase, lavandulyl diphosphate synthase (LPPS). LPPS catalyzes the condensation of two molecules of dimethylallyl diphosphate (DMAPP) to form lavandulyl diphosphate, a precursor to the fragrance lavandulol. The structure is similar to that of the bacterial cis-prenyl synthase, undecaprenyl diphosphate synthase (UPPS), and contains an allylic site (S1) in which DMAPP ionizes and a second site (S2) which houses the DMAPP nucleophile. Both S-thiolo-dimethylallyl diphosphate and S-thiolo-isopentenyl diphosphate bind intact to S2, but are cleaved to (thio)diphosphate, in S1. His78 (Asn in UPPS) is essential for catalysis and is proposed to facilitate diphosphate release in S1, while the P1 phosphate in S2 abstracts a proton from the lavandulyl carbocation to form the LPP product. The results are of interest since they provide the first structure and structure-based mechanism of this unusual prenyl synthase. Structure and Function of a "Head-to-Middle" Prenyltransferase: Lavandulyl Diphosphate Synthase.,Liu M, Chen CC, Chen L, Xiao X, Zheng Y, Huang JW, Liu W, Ko TP, Cheng YS, Feng X, Oldfield E, Guo RT, Ma Y Angew Chem Int Ed Engl. 2016 Apr 4;55(15):4721-4. doi: 10.1002/anie.201600656., Epub 2016 Feb 29. PMID:26922900[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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