Campus Units

Biochemistry, Biophysics and Molecular Biology, Roy J. Carver Department of

Document Type

Article

Publication Version

Accepted Manuscript

Publication Date

8-15-2010

Journal or Book Title

Proteins

Volume

78

Issue

11

First Page

2417

Last Page

2432

DOI

10.1002/prot.22751

Abstract

The structures and mechanism of action of many terpene cyclases are known, but there are no structures of diterpene cyclases. Here, we propose structural models based on bioinformatics, sitedirected mutagenesis, domain swapping, enzyme inhibition and spectroscopy that help explain the nature of diterpene cyclase structure, function, and evolution. Bacterial diterpene cyclases contain ～20 α-helices and the same conserved “QW” and DxDD motifs as in triterpene cyclases, indicating the presence of a βγ barrel structure. Plant diterpene cyclases have a similar catalytic motif and βγ-domain structure together with a third, α-domain, forming an αβγ structure, and in H+-initiated cyclases, there is an EDxxD-like Mg2+/diphosphate binding motif located in the γ- domain. The results support a new view of terpene cyclase structure and function and suggest evolution from ancient (βγ) bacterial triterpene cyclases to (βγ) bacterial and thence to (αβγ) plant

Comments

This is the peer reviewed version of the following article: Cao, R., Zhang, Y., Mann, F. M., Huang, C., Mukkamala, D., Hudock, M. P., Mead, M. E., Prisic, S., Wang, K., Lin, F.-Y., Chang, T.-K., Peters, R. J. and Oldfield, E. (2010), Diterpene cyclases and the nature of the isoprene fold. Proteins, 78: 2417–2432, which has been published in final form at doi:10.1002/prot.22751. This article may be used for non-commercial purposes in accordance With Wiley Terms and Conditions for self-archiving.

Copyright Owner

Wiley-Liss, Inc.

Language

en

File Format

application/pdf

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