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Plants produce a wide variety of secondary metabolites in response to adverse environmental factors. Z , Z -Farnesyl diphosphate ( Z , Z -FPP), synthesized by Z , Z -farnesyl diphosphate synthase ( z FPS), supports the formation of phytochemicals in wild tomatoes. Here, the crystal structure of N-terminal truncated z FPS (Δ z FPS) was determined. Irregular products including lavandulyl diphosphate and an unknown compound were surprisingly found. Apart from the truncated N-terminus as a functional regulator, structure-based analysis and mutagenesis assays revealed a residue H103 in Δ z FPS as one of the key elements to this irregular function. A series of substrate-enzyme complex structures were obtained from Δ z FPS-H103Y by co-crystallizing with isopentenyl diphosphate, dimethylallyl thiolodiphosphate, or both. Various substrate-binding modes were revealed. The catalytic mechanisms of both the head-to-tail and head-to-middle reactions in Δ z FPS were proposed. Functional switch between the two mechanisms in this enzyme and the essential role played by the flexible C-terminus were elucidated as well.

Crystal Structure and Potential Head-to-Middle Condensation Function of a Z,Z-Farnesyl Diphosphate Synthase