Micrococcin cysteine-to-thiazole conversion through transient interactions between a scaffolding protein and two modification enzymes.

ABSTRACT: Ribosomally synthesized and post-translationally modified peptides (RiPPs) are a broad group of compounds mediating microbial competition in nature. Azole/azoline heterocycle formation in the peptide backbone is a key step in the biosynthesis of many RiPPs. Heterocycle formation in RiPP precursors is often carried out by a scaffold protein, an ATP-dependent cyclodehydratase, and an FMN-dependent dehydrogenase. It has generally been assumed that the orchestration of these modifications is carried out by a stable complex including the scaffold, cyclodehydratase and dehydrogenase. The antimicrobial RiPP micrococcin begins as a precursor peptide (TclE) with a 35-amino acid N-terminal leader and a 14-amino acid C-terminal core containing six Cys residues that are converted to thiazoles. The put

SUBMITTER: Calvopina-Chavez DG 

PROVIDER: S-EPMC10634744 | biostudies-literature | 2023 Oct

REPOSITORIES: biostudies-literature