Campus Units

Biochemistry, Biophysics and Molecular Biology

Document Type

Article

Publication Version

Accepted Manuscript

Publication Date

2011

Journal or Book Title

Nature Chemical Biology

Volume

7

Issue

7

First Page

431

Last Page

433

DOI

10.1038/nchembio.578

Abstract

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.

Comments

This is a manuscript of an article published as Köksal, Mustafa, Huayou Hu, Robert M. Coates, Reuben J. Peters, and David W. Christianson. "Structure and mechanism of the diterpene cyclase ent-copalyl diphosphate synthase." Nature chemical biology 7, no. 7 (2011): 431-433. doi: 10.1038/nchembio.578. Posted with permission.

Copyright Owner

Nature Publishing Group

Language

en

File Format

application/pdf

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