Elshahawi, Sherif I.Cao, HongnanShaaban, Khaled A.Ponomareva, Larissa V.Subramanian, ThangaiahFarman, Mark L.Spielmann, H.PeterPhillips, George N.Jr.Thorson, Jon S.Singh, Shanteri2017-08-092017-08-092017Elshahawi, Sherif I., Cao, Hongnan, Shaaban, Khaled A., et al.. "Structure and specificity of a permissive bacterial C-prenyltransferase." <i>Nature Chemical Biology,</i> 13, (2017) Springer Nature: 366-368. https://doi.org/10.1038/nchembio.2285.https://hdl.handle.net/1911/96641This 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.engThis is an author's peer-reviewed final manuscript, as accepted by the publisher. The published article is copyrighted by Springer Nature.Structure and specificity of a permissive bacterial C-prenyltransferaseJournal articleStructure-and-Specificityhttps://doi.org/10.1038/nchembio.2285