Official Project Description
Lanthipeptides are ribosomally synthesized and post-translationally modified peptides that are generated from precursor peptides through a dehydration and cyclization process.
Lanthipeptides have demonstrated a variety of bioactivities, including anticancer, antimicrobial, antiviral, and antiallodynic activities.
ProcM, a class II lanthipeptide synthetase, demonstrates high substrate tolerance.
It is enigmatic that a single enzyme can catalyze the cyclization process of many substrates with high fidelity.
This feature has been widely utilized for bioengineering of novel lanthipeptides.
However, the molecular mechanism about how ProcM determines site-selectivity of its substrates is still unclear.
In this study, we would like to run atomic-level MD simulation for WT and Variant ProcM-ProcA3.3 complex to explore the site-selectivity of ProcM.