3s9v: Difference between revisions

Latest revision as of 09:48, 1 March 2024

abietadiene synthase from Abies grandis

Structural highlights

3s9v is a 4 chain structure with sequence from Abies grandis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.3Å
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

TPSDV_ABIGR Involved in defensive oleoresin formation in conifers in response to insect attack or other injury. Involved in diterpene (C20) olefins biosynthesis. Bifunctional enzyme that catalyzes two sequential cyclizations of geranylgeranyl diphosphate (GGPP) to abietadiene. The copalyl diphosphate (CPP) intermediate diffuses freely between the 2 active sites in the enzyme. Changes in reaction pH, but not salt concentration, influence the relative proportion of the major products of the enzyme, abitadiene, levopimaradiene and neoabitadiene.^[1] ^[2] ^[3] ^[4] ^[5] ^[6] ^[7]

References

↑ Bohlmann J, Meyer-Gauen G, Croteau R. Plant terpenoid synthases: molecular biology and phylogenetic analysis. Proc Natl Acad Sci U S A. 1998 Apr 14;95(8):4126-33. PMID:9539701
↑ Peters RJ, Flory JE, Jetter R, Ravn MM, Lee HJ, Coates RM, Croteau RB. Abietadiene synthase from grand fir (Abies grandis): characterization and mechanism of action of the "pseudomature" recombinant enzyme. Biochemistry. 2000 Dec 19;39(50):15592-602. PMID:11112547
↑ Ravn MM, Coates RM, Flory JE, Peters RJ, Croteau R. Stereochemistry of the cyclization-rearrangement of (+)-copalyl diphosphate to (-)-abietadiene catalyzed by recombinant abietadiene synthase from Abies grandis. Org Lett. 2000 Mar 9;2(5):573-6. PMID:10814381
↑ Peters RJ, Croteau RB. Abietadiene synthase catalysis: conserved residues involved in protonation-initiated cyclization of geranylgeranyl diphosphate to (+)-copalyl diphosphate. Biochemistry. 2002 Feb 12;41(6):1836-42. PMID:11827528
↑ Peters RJ, Carter OA, Zhang Y, Matthews BW, Croteau RB. Bifunctional abietadiene synthase: mutual structural dependence of the active sites for protonation-initiated and ionization-initiated cyclizations. Biochemistry. 2003 Mar 11;42(9):2700-7. PMID:12614165 doi:https://dx.doi.org/10.1021/bi020492n
↑ Wilderman PR, Peters RJ. A single residue switch converts abietadiene synthase into a pimaradiene specific cyclase. J Am Chem Soc. 2007 Dec 26;129(51):15736-7. Epub 2007 Dec 1. PMID:18052062 doi:https://dx.doi.org/10.1021/ja074977g
↑ Mann FM, Prisic S, Davenport EK, Determan MK, Coates RM, Peters RJ. A single residue switch for Mg(2+)-dependent inhibition characterizes plant class II diterpene cyclases from primary and secondary metabolism. J Biol Chem. 2010 Jul 2;285(27):20558-63. doi: 10.1074/jbc.M110.123307. Epub 2010, Apr 29. PMID:20430888 doi:10.1074/jbc.M110.123307

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OCA

[1] Bohlmann J, Meyer-Gauen G, Croteau R. Plant terpenoid synthases: molecular biology and phylogenetic analysis. Proc Natl Acad Sci U S A. 1998 Apr 14;95(8):4126-33. PMID:9539701

[2] Peters RJ, Flory JE, Jetter R, Ravn MM, Lee HJ, Coates RM, Croteau RB. Abietadiene synthase from grand fir (Abies grandis): characterization and mechanism of action of the "pseudomature" recombinant enzyme. Biochemistry. 2000 Dec 19;39(50):15592-602. PMID:11112547

[3] Ravn MM, Coates RM, Flory JE, Peters RJ, Croteau R. Stereochemistry of the cyclization-rearrangement of (+)-copalyl diphosphate to (-)-abietadiene catalyzed by recombinant abietadiene synthase from Abies grandis. Org Lett. 2000 Mar 9;2(5):573-6. PMID:10814381

[4] Peters RJ, Croteau RB. Abietadiene synthase catalysis: conserved residues involved in protonation-initiated cyclization of geranylgeranyl diphosphate to (+)-copalyl diphosphate. Biochemistry. 2002 Feb 12;41(6):1836-42. PMID:11827528

[5] Peters RJ, Carter OA, Zhang Y, Matthews BW, Croteau RB. Bifunctional abietadiene synthase: mutual structural dependence of the active sites for protonation-initiated and ionization-initiated cyclizations. Biochemistry. 2003 Mar 11;42(9):2700-7. PMID:12614165 doi:https://dx.doi.org/10.1021/bi020492n

[6] Wilderman PR, Peters RJ. A single residue switch converts abietadiene synthase into a pimaradiene specific cyclase. J Am Chem Soc. 2007 Dec 26;129(51):15736-7. Epub 2007 Dec 1. PMID:18052062 doi:https://dx.doi.org/10.1021/ja074977g

[7] Mann FM, Prisic S, Davenport EK, Determan MK, Coates RM, Peters RJ. A single residue switch for Mg(2+)-dependent inhibition characterizes plant class II diterpene cyclases from primary and secondary metabolism. J Biol Chem. 2010 Jul 2;285(27):20558-63. doi: 10.1074/jbc.M110.123307. Epub 2010, Apr 29. PMID:20430888 doi:10.1074/jbc.M110.123307

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@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 3s9v is ON HOLD
+==abietadiene synthase from Abies grandis==
+<StructureSection load='3s9v' size='340' side='right'caption='[[3s9v]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
-Authors: Zhou, k, Hoy, J.A., Mann, F.M., Honzatko, R.B., Peters, R.J.
+== Structural highlights ==
+<table><tr><td colspan='2'>[[3s9v]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Abies_grandis Abies grandis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3S9V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3S9V FirstGlance]. <br>
-Description: abietadiene synthase from Abies grandis
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3&#8491;</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=3s9v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3s9v OCA], [https://pdbe.org/3s9v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3s9v RCSB], [https://www.ebi.ac.uk/pdbsum/3s9v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3s9v ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/TPSDV_ABIGR TPSDV_ABIGR] Involved in defensive oleoresin formation in conifers in response to insect attack or other injury. Involved in diterpene (C20) olefins biosynthesis. Bifunctional enzyme that catalyzes two sequential cyclizations of geranylgeranyl diphosphate (GGPP) to abietadiene. The copalyl diphosphate (CPP) intermediate diffuses freely between the 2 active sites in the enzyme. Changes in reaction pH, but not salt concentration, influence the relative proportion of the major products of the enzyme, abitadiene, levopimaradiene and neoabitadiene.<ref>PMID:9539701</ref> <ref>PMID:11112547</ref> <ref>PMID:10814381</ref> <ref>PMID:11827528</ref> <ref>PMID:12614165</ref> <ref>PMID:18052062</ref> <ref>PMID:20430888</ref>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Abies grandis]]
+[[Category: Large Structures]]
+[[Category: Honzatko RB]]
+[[Category: Hoy JA]]
+[[Category: Mann FM]]
+[[Category: Peters RJ]]
+[[Category: Zhou K]]

3s9v: Difference between revisions

Latest revision as of 09:48, 1 March 2024

abietadiene synthase from Abies grandis

Structural highlights

Function

References

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