Structure and mechanism of the diterpene cyclase ent-copalyl diphosphate synthase
- UIUC
The structure of ent-copalyl diphosphate synthase reveals three {alpha}-helical domains ({alpha}, {beta} and {gamma}), as also observed in the related diterpene cyclase taxadiene synthase. However, active sites are located at the interface of the {beta}{gamma} domains in ent-copalyl diphosphate synthase but exclusively in the {alpha} 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.
- Research Organization:
- Advanced Photon Source (APS), Argonne National Laboratory (ANL), Argonne, IL (US)
- Sponsoring Organization:
- NIH
- OSTI ID:
- 1023674
- Journal Information:
- Nat. Chem. Biol., Journal Name: Nat. Chem. Biol. Journal Issue: 07, 2011 Vol. 7
- Country of Publication:
- United States
- Language:
- ENGLISH
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