Structures of the peptide-modifying radical SAM enzyme SuiB elucidate the basis of substrate recognition.

ABSTRACT: Posttranslational modification of ribosomally synthesized peptides provides an elegant means for the production of biologically active molecules known as RiPPs (ribosomally synthesized and posttranslationally modified peptides). Although the leader sequence of the precursor peptide is often required for turnover, the exact mode of recognition by the modifying enzymes remains unclear for many members of this class of natural products. Here, we have used X-ray crystallography and computational modeling to examine the role of the leader peptide in the biosynthesis of a homolog of streptide, a recently identified peptide natural product with an intramolecular lysine-tryptophan cross-link, which is installed by the radical S-adenosylmethionine (SAM) enzyme, StrB. We present crystal struc

SUBMITTER: Davis KM 

PROVIDER: S-EPMC5625900 | biostudies-literature | 2017 Sep

REPOSITORIES: biostudies-literature