2q9y | pdb_00002q9y
Trichodiene synthase: Complex with Mg, inorganic pyrophosphate, and benzyl triethyl ammonium cation
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
2Q9Y is a Single protein structure of sequence from Fusarium sporotrichioides. 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 Page seeded by OCA on Thu Apr 24 09:40:27 2008
