Structure and mechanism of the diterpene cyclase ent-copalyl diphosphate synthase.

Publication Type:

Journal Article

Authors:

Köksal, Mustafa; Hu, Huayou; Coates, Robert M; Peters, Reuben J; Christianson, David W

Source:

Nat Chem Biol, Volume 7, Issue 7, p.431-3 (2011)

Keywords:

Alkyl and Aryl Transferases, Amino Acid Motifs, Amino Acid Sequence, Catalysis, Catalytic Domain, Crystallography, X-Ray, Cyclization, Evolution, Molecular, Isomerases, Models, Molecular, Molecular Sequence Data, Molecular Structure, Organophosphates, Plant Proteins, Protein Binding, Protein Structure, Tertiary, Sequence Alignment, Sesquiterpenes, Terpenes

Abstract:

<p>The structure of ent-copalyl diphosphate synthase reveals three α-helical domains (α, β and γ), as also observed in the related diterpene cyclase taxadiene synthase. However, active sites are located at the interface of the βγ domains in ent-copalyl diphosphate synthase 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.</p>