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.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Anti-Infective Agents / metabolism*
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Anti-Infective Agents / pharmacology
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Bacterial Outer Membrane Proteins / metabolism*
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Bacteriocins / metabolism*
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Endocytosis
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Escherichia coli / metabolism
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Escherichia coli Proteins / metabolism
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Models, Molecular
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Protein Conformation
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Receptors, Cell Surface / metabolism*
Substances
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Anti-Infective Agents
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Bacterial Outer Membrane Proteins
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Bacteriocins
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Escherichia coli Proteins
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FhuA protein, E coli
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Receptors, Cell Surface
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siderophore receptors
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microcin