Cyanobactins are ribosomally synthesized and post-translationally modified cyclic peptides produced by various symbiontic or independent cyanobacteria. Analysis of cyanobactins and their biosynthetic gene clusters demonstrates that several cyanobactins are prenylated, and subsequent biochemical studies characterize the putative prenyltransferases. In prenylagaramides biosynthesis, PagF is the prenyltransferase that can transfer a prenyl group in vitro from dimethylallyl pyrophosphate to the O of Tyr, only in the context of a cyclic peptide. In order to understand this unexpected substrate regiospecificity, and to provide a mechanistic understanding of prenylation by this new class of prenyltransferases, I have solved the crystal structure of PagF with the prenyl group donor analog. I will discuss its overall structure and the interactions between the protein and its substrate.

Structural studies of the prenyltransferase involved in cyanobactin biosynthesis

246th National Meeting (2013)

The official archive and repository for all ACS Meetings & Expositions abstracts and select posters or presentations.