Structural determinants of macrocyclization in substrate-controlled lanthipeptide biosynthetic pathways.

ABSTRACT: Lanthipeptides are characterized by thioether crosslinks formed by post-translational modifications. The cyclization process that favors a single ring pattern over many other possible ring patterns has been the topic of much speculation. Recent studies suggest that for some systems the cyclization pattern and stereochemistry is determined not by the enzyme, but by the sequence of the precursor peptide. However, the factors that govern the outcome of the cyclization process are not understood. This study presents the three-dimensional structures of seven lanthipeptides determined by nuclear magnetic resonance spectroscopy, including five prochlorosins and the two peptides that make up cytolysin, a virulence factor produced by Enterococcus faecalis that is directly linked to human dis

SUBMITTER: Bobeica SC 

PROVIDER: S-EPMC8163290 | biostudies-literature | 2020 Jun

REPOSITORIES: biostudies-literature