This study highlights the biochemical and structural characterization of the L-tryptophan C6 C-prenyltransferase (C-PT) PriB from Streptomyces sp. RM-5-8. PriB was found to be uniquely permissive to a diverse array of prenyl donors and acceptors including daptomycin. Two additional PTs also produced novel prenylated daptomycins with improved antibacterial activities over the parent drug.

Document Type


Publication Date


Notes/Citation Information

Published in Nature Chemical Biology, v. 13, issue 4, p. 366-368.

© 2017 Nature America, Inc., part of Springer Nature. All rights reserved.

The copyright holder has granted the permission for posting the article here.

This is a post-peer-review, pre-copyedit version of an article published in Nature Chemical Biology. The final authenticated version is available online at: https://doi.org/10.1038/nchembio.2285.

Digital Object Identifier (DOI)


Funding Information

This work was supported by NIH grants R37 AI52188 and R01 CA203257 (J.S.T.), U01 GM098248 (G.N.P.) and NCATS (UL1TR001998).

Related Content

Supplementary information and chemical compound information is available online at http://www.nature.com/naturechemicalbiology/.

Nucleotide sequence data for pri cluster is available under GenBank accession code KT895008. The PriB X-ray crystal structures were deposited at the Protein Database Bank: PriB/L-Trp/dimethylallyl S-thiolodiphosphate ternary complex (5INJ), the apo structure (5JXM), and the PriB/pyrophosphate binary complex (5K9M). All other data generated or analyzed during this study are included in this published article (and its supplementary information files) or are available from the corresponding author on reasonable request.

nchembio.2285-S1.pdf (2642 kB)
Supplementary Text and Figures

nchembio.2285-S2.pdf (15278 kB)
Supplementary Note