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Structural basis for hijacking siderophore receptors by antimicrobial lasso peptides

The lasso peptide microcin J25 is known to hijack the siderophore receptor FhuA for initiating internalization. Here, we provide the first structural evidence on the recognition mechanism and our biochemical data show that another closely related lasso peptide cannot interact with FhuA. Our work pro...

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Detalles Bibliográficos
Autores principales: Mathavan, Indran, Zirah, Séverine, Mehmood, Shahid, Choudhury, Hassanul G., Goulard, Christophe, Li, Yanyan, Robinson, Carol V., Rebuffat, Sylvie, Beis, Konstantinos
Formato: Online Artículo Texto
Lenguaje:English
Publicado: 2014
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3992131/
https://www.ncbi.nlm.nih.gov/pubmed/24705590
http://dx.doi.org/10.1038/nchembio.1499
Descripción
Sumario:The lasso peptide microcin J25 is known to hijack the siderophore receptor FhuA for initiating internalization. Here, we provide the first structural evidence on the recognition mechanism and our biochemical data show that another closely related lasso peptide cannot interact with FhuA. Our work provides an explanation on the narrow activity spectrum of lasso peptides and opens the path to the development of new antibacterials.