Lantibiotics are antibiotic peptides distinguished by the presence of the rare 
thioether amino acids lanthionine and/or methyllanthionine. They are produced by 
Gram-positive bacteria as gene-encoded precursor peptides and undergo 
post-translational modification to generate the mature peptide. The structural 
gene for the prepeptide and the genes involved in biosynthesis, processing, 
export as well as regulation and producer strain self-protection are organized 
in clusters. Based on their structural and functional features lantibiotics are 
currently divided into two major groups. The flexible amphiphilic type-A 
lantibiotics act primarily by pore formation in the bacterial membrane, a 
mechanism which was recently shown, e.g. for nisin and epidermin, to involve the 
interaction with specific docking molecules such as the membrane precursor lipid 
II. The rather rigid and globular type-B lantibiotics inhibit enzyme functions 
through interaction with the respective substrates: mersacidin and actagardine 
inhibit the cell wall biosynthesis by complexing lipid II, whereas the 
cinnamycin-like peptides inhibit phospholipases by binding phosphoethanolamine. 
Lantibiotics have attracted much attention in recent years and undergone 
extensive characterization. New insights into the mode of action and 
structure-function relationships as well as the biochemistry and the genetics 
will be outlined in this review.