Fusicoccadiene synthase is responsible for producing the precursor of fusicoccin A, a plant wilting toxin and chemotherapeutic compound. Fusicoccadiene synthase is a bifunctional diterpene synthase with an alpha-alpha fold, catalyzing sequential terpene elongation and cyclization reactions. Herein, we present the crystal structures of each individual alpha domains and small angle x-ray scattering analysis of full-length fusicoccadiene synthase, along with biochemical characterization to elucidate its structural-functional relationship. The fusion of elongation domain to cyclization domain not only ensures product specificity, but also accelerates catalysis by creating spatial proximity of two domains. The active site of cyclization domain displays unprecedented feature that presumably participates in mediating enzymatic activity. Intriguingly, we have discovered that cyclization by full-length PaFS is subject to allosteric regulation. Together, these results reveal previously unknown strategies involved in terpene biosynthesis.<br/>

Structure and function of fusicoccadiene synthase, a bifunctional diterpene synthase with an alpha-alpha fold

251st National Meeting (2016)

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