Disordered regions in proteusin peptides guide post-translational modification by a flavin-dependent RiPP brominase.

ABSTRACT: To biosynthesize ribosomally synthesized and post-translationally modified peptides (RiPPs), 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 are RiPP precursor peptides that defy this characterization as they possess unusually long leaders. Proteusin peptides have not been structurally characterized, and we possess scant understanding of how these atypical leaders engage with modifying enzymes. Here, we determine the structure of a proteusin peptide which shows that unlike other RiPP leaders, proteusin leaders are preorganized into a rigidly structured region and a smaller intrinsically disordered

SUBMITTER: Nguyen NA 

PROVIDER: S-EPMC10858898 | biostudies-literature | 2024 Feb

REPOSITORIES: biostudies-literature