In:
Scientific Reports, Springer Science and Business Media LLC, Vol. 6, No. 1 ( 2016-01-04)
Abstract:
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 ( Sa NSR) at 2.2 Å 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 Sa NSR/nisin complex is generated, revealing that Sa NSR recognizes the last C-terminally located lanthionine ring of nisin. This determines the substrate specificity of Sa NSR and ensures the exact coordination of the nisin cleavage site at the TASSAEM region.
Type of Medium:
Online Resource
ISSN:
2045-2322
Language:
English
Publisher:
Springer Science and Business Media LLC
Publication Date:
2016
detail.hit.zdb_id:
2615211-3
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