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. 2021 Jan 27;48(3-4):kuab005. doi: 10.1093/jimb/kuab005

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© The Author(s) 2021. Published by Oxford University Press on behalf of Society of Industrial Microbiology and Biotechnology.

This is an Open Access article distributed under the terms of the Creative Commons Attribution License (https://creativecommons.org/licenses/by/4.0/), which permits unrestricted reuse, distribution, and reproduction in any medium, provided the original work is properly cited.

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Fig. 3. — Structure and mechanism of action of the lanthipeptide nisin. (A) Representation of nisin structure. Dhb: dehydrobutyrine, Dha: dehydroalanine, Abu: aminobutyric acid. The thioether linkage between Ala and Ala is referred to as a lanthionine moiety while the linkage between Abu and Ala is a methyllanthionine linkage. (B) NMR structure (PDB file 1WCO) of nisin bound to a lipid II analog. Nisin is shown as a space-filling model and the lipid II analog is shown as sticks. The N-terminal (methyl)lanthionine rings (space-filling tan) of nisin envelop the pyrophosphate moiety (magenta and cyan sticks) of lipid II.