NHLP leader peptide family natural product (I56V)

The protein construct used for SXS contains a non-native C-terminal extension (LTVLPW) and a I56V point mutation. To biosynthesize ribosomally synthesized and post-translationally modified peptides (RiPPs), modifying enzymes recognize and bind to the N-terminal leader region of substrate peptides which enables catalytic modification of the C-terminal core. Our current understanding of RiPP leaders is that they are short and largely unstructured. Proteusins, widely encoded in bacterial genomes, are RiPP precursor peptides that defy this characterization as they possess unusually long leaders.