2q9z

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(New page: 200px<br /><applet load="2q9z" size="350" color="white" frame="true" align="right" spinBox="true" caption="2q9z, resolution 2.95&Aring;" /> '''Trichodiene synthase...)
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==Overview==
==Overview==
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Trichodiene synthase is a terpenoid cyclase that catalyzes the cyclization, of farnesyl diphosphate (FPP) to form the bicyclic sesquiterpene, hydrocarbon trichodiene (89%), at least five sesquiterpene side products, (11%), and inorganic pyrophosphate (PP(i)). Incubation of trichodiene, synthase with 2-fluorofarnesyl diphosphate or 4-methylfarnesyl diphosphate, similarly yields sesquiterpene mixtures despite the electronic effects or, steric bulk introduced by substrate derivatization. The versatility of the, enzyme is also demonstrated in the 2.85A resolution X-ray crystal, structure of the complex with Mg(2+) (3)-PP(i) and the benzyl, triethylammonium cation, which is a bulkier mimic of the bisabolyl, carbocation intermediate in catalysis. Taken together, these findings show, that the active site of trichodiene synthase is sufficiently flexible to, accommodate bulkier and electronically-diverse substrates and, intermediates, which could indicate additional potential for the, biosynthetic utility of this terpenoid cyclase.
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Trichodiene synthase is a terpenoid cyclase that catalyzes the cyclization of farnesyl diphosphate (FPP) to form the bicyclic sesquiterpene hydrocarbon trichodiene (89%), at least five sesquiterpene side products (11%), and inorganic pyrophosphate (PP(i)). Incubation of trichodiene synthase with 2-fluorofarnesyl diphosphate or 4-methylfarnesyl diphosphate similarly yields sesquiterpene mixtures despite the electronic effects or steric bulk introduced by substrate derivatization. The versatility of the enzyme is also demonstrated in the 2.85A resolution X-ray crystal structure of the complex with Mg(2+) (3)-PP(i) and the benzyl triethylammonium cation, which is a bulkier mimic of the bisabolyl carbocation intermediate in catalysis. Taken together, these findings show that the active site of trichodiene synthase is sufficiently flexible to accommodate bulkier and electronically-diverse substrates and intermediates, which could indicate additional potential for the biosynthetic utility of this terpenoid cyclase.
==About this Structure==
==About this Structure==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Trichodiene synthase]]
[[Category: Trichodiene synthase]]
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[[Category: Cane, D.E.]]
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[[Category: Cane, D E.]]
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[[Category: Christianson, D.W.]]
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[[Category: Christianson, D W.]]
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[[Category: Coates, R.M.]]
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[[Category: Coates, R M.]]
[[Category: Koyama, T.]]
[[Category: Koyama, T.]]
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[[Category: Vedula, L.S.]]
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[[Category: Vedula, L S.]]
[[Category: Zhao, Y.]]
[[Category: Zhao, Y.]]
[[Category: EDO]]
[[Category: EDO]]
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[[Category: terpenoid synthase fold]]
[[Category: terpenoid synthase fold]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 12:37:17 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:37:31 2008''

Revision as of 16:37, 21 February 2008


2q9z, resolution 2.95Å

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Trichodiene synthase: Complex with inorganic pyrophosphate resulting from the reaction with 2-fluorofarnesyl diphosphate

Overview

Trichodiene synthase is a terpenoid cyclase that catalyzes the cyclization of farnesyl diphosphate (FPP) to form the bicyclic sesquiterpene hydrocarbon trichodiene (89%), at least five sesquiterpene side products (11%), and inorganic pyrophosphate (PP(i)). Incubation of trichodiene synthase with 2-fluorofarnesyl diphosphate or 4-methylfarnesyl diphosphate similarly yields sesquiterpene mixtures despite the electronic effects or steric bulk introduced by substrate derivatization. The versatility of the enzyme is also demonstrated in the 2.85A resolution X-ray crystal structure of the complex with Mg(2+) (3)-PP(i) and the benzyl triethylammonium cation, which is a bulkier mimic of the bisabolyl carbocation intermediate in catalysis. Taken together, these findings show that the active site of trichodiene synthase is sufficiently flexible to accommodate bulkier and electronically-diverse substrates and intermediates, which could indicate additional potential for the biosynthetic utility of this terpenoid cyclase.

About this Structure

2Q9Z is a Single protein structure of sequence from Fusarium sporotrichioides with , and as ligands. Active as Trichodiene synthase, with EC number 4.2.3.6 Full crystallographic information is available from OCA.

Reference

Exploring biosynthetic diversity with trichodiene synthase., Vedula LS, Zhao Y, Coates RM, Koyama T, Cane DE, Christianson DW, Arch Biochem Biophys. 2007 Oct 15;466(2):260-6. Epub 2007 Jun 28. PMID:17678871

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