Steric complementarity directs sequence promiscuous leader binding in RiPP biosynthesis.

ABSTRACT: Enzymes that generate ribosomally synthesized and posttranslationally modified peptide (RiPP) natural products have garnered significant interest, given their ability to produce large libraries of chemically diverse scaffolds. Such RiPP biosynthetic enzymes are predicted to bind their corresponding peptide substrates through sequence-specific recognition of the leader sequence, which is removed after the installation of posttranslational modifications on the core sequence. The conservation of the leader sequence within a given RiPP class, in otherwise disparate precursor peptides, further supports the notion that strict sequence specificity is necessary for leader peptide engagement. Here, we demonstrate that leader binding by a biosynthetic enzyme in the lasso peptide class of RiPPs is di

SUBMITTER: Chekan JR 

PROVIDER: S-EPMC6883790 | biostudies-literature | 2019 Nov

REPOSITORIES: biostudies-literature