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Structural basis for hijacking siderophore receptors by antimicrobial lasso peptides.

ABSTRACT: The lasso peptide microcin J25 is known to hijack the siderophore receptor FhuA for initiating internalization. Here, we provide what is to our knowledge 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.

SUBMITTER: Mathavan I

PROVIDER: S-EPMC3992131 | biostudies-literature | 2014 May

REPOSITORIES: biostudies-literature

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Structural basis for hijacking siderophore receptors by antimicrobial lasso peptides.

Mathavan Indran I Zirah Séverine S Mehmood Shahid S Choudhury Hassanul G HG Goulard Christophe C Li Yanyan Y Robinson Carol V CV Rebuffat Sylvie S Beis Konstantinos K

Nature chemical biology 20140406 5

The lasso peptide microcin J25 is known to hijack the siderophore receptor FhuA for initiating internalization. Here, we provide what is to our knowledge 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. ...[more]

PMID: 24705590

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