Structural highlights
Publication Abstract from PubMed
Lantibiotics are potent antimicrobial peptides. Nisin is the most prominent member and contains five crucial lanthionine rings. Some clinically relevant bacteria express membrane-associated resistance proteins that proteolytically inactivate nisin. However, substrate recognition and specificity of these proteins is unknown. Here, we report the first three-dimensional structure of a nisin resistance protein from Streptococcus agalactiae (SaNSR) at 2.2 A resolution. It contains an N-terminal helical bundle, and protease cap and core domains. The latter harbors the highly conserved TASSAEM region, which lies in a hydrophobic tunnel formed by all domains. By integrative modeling, mutagenesis studies, and genetic engineering of nisin variants, a model of the SaNSR/nisin complex is generated, revealing that SaNSR recognizes the last C-terminally located lanthionine ring of nisin. This determines the substrate specificity of SaNSR and ensures the exact coordination of the nisin cleavage site at the TASSAEM region.
Structural basis of lantibiotic recognition by the nisin resistance protein from Streptococcus agalactiae.,Khosa S, Frieg B, Mulnaes D, Kleinschrodt D, Hoeppner A, Gohlke H, Smits SH Sci Rep. 2016 Jan 4;6:18679. doi: 10.1038/srep18679. PMID:26727488[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Khosa S, Frieg B, Mulnaes D, Kleinschrodt D, Hoeppner A, Gohlke H, Smits SH. Structural basis of lantibiotic recognition by the nisin resistance protein from Streptococcus agalactiae. Sci Rep. 2016 Jan 4;6:18679. doi: 10.1038/srep18679. PMID:26727488 doi:http://dx.doi.org/10.1038/srep18679
