Fig. 4
From: Unveiling the biosynthesis mechanism of novel lantibiotic homicorcin: an in silico analysis
Representation of the protein-protein docking complex and interacting residues of dehydrated HomA-HomC (A), cyclized HomA-HomT (B), and cyclized HomA-HomP (C). Conserved residues of HomC and NisC catalytic sites (D). His212, Arg280, Cys284, Cys330, and His331 of NisC are situated in its catalytic site, playing crucial roles in pre-NisA cyclization. Cys284, Cys330, and His331 of NisC stabilize a zinc ion that activates the thiol group of pre-NisA Cys residues, followed by its deprotonation. His212 and Arg280 involve removing the proton from the Cys residue and adding a proton to the enolate intermediate formed by conjugate addition to the β carbon of Dha/Dhb, ultimately facilitating the cyclization reaction in NisC. Conservation of these residues in HomC may function similarly in HomA cyclization (E).
