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.
Copyright Owner
Nature Publishing Group
Copyright Date
2011
Language
en
File Format
application/pdf
Recommended Citation
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.
https://lib.dr.iastate.edu/bbmb_ag_pubs/107
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.