Official Project Description
Lanthipeptides are a class of ribosomally synthesized and post-translationally modified peptides (RiPPs) produced from precursor peptides through dehydration and cyclization reactions.
They exhibit a broad range of bioactivities, including anticancer, antimicrobial, antiviral, and antiallodynic effects.
ProcM, a class II lanthipeptide synthetase, is notable for its high substrate tolerance.
Remarkably, this single enzyme can catalyze the cyclization of a diverse array of substrates with high fidelityâ€â€an ability that has been extensively leveraged in the bioengineering of novel lanthipeptides.
Despite this, the molecular mechanism by which ProcM determines the site-selectivity of its substrates remains unclear.
In this study, we aim to perform atomic-level molecular dynamics (MD) simulations of the wild-type (WT) and Variant ProcM–ProcA3.3 complexes to investigate the basis of ProcM's site-selectivity.