Biochemistry, Biophysics and Molecular Biology, Roy J. Carver Department of
Journal or Book Title
Nature Chemical Biology
The structure of ent-copalyl diphosphate synthase (CPS) reveals three α-helical domains (α, β, γ), as also observed in the related diterpene cyclase taxadiene synthase. However, active sites are located at the interface of the βγ domains in CPS but exclusively in the α domain of taxadiene synthase. Modular domain architecture in plant diterpene cyclases enables the evolution of alternative active sites and chemical strategies for catalyzing isoprenoid cyclization reactions.
Nature Publishing Group
Köksal, Mustafa; Hu, Huayou; Coates, Robert M.; Peters, Reuben J.; and Christianson, David D., "Structure and mechanism of the diterpene cyclase ent-copalyl diphosphate synthase" (2011). Biochemistry, Biophysics and Molecular Biology Publications. 107.