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Nat Chem Biol. 2014 May;10(5):340-2. doi: 10.1038/nchembio.1499. Epub 2014 Apr 6.

Structural basis for hijacking siderophore receptors by antimicrobial lasso peptides.

Author information

1
1] Department of Life Sciences, Imperial College London, London, UK. [2] Membrane Protein Lab, Diamond Light Source, Harwell Science and Innovation Campus, Chilton, Oxfordshire, UK. [3] Rutherford Appleton Laboratory, Research Complex at Harwell, Didcot, Oxfordshire, UK.
2
Communication Molecules and Adaptation of Microorganisms Laboratory, UMR 7245 CNRS-Muséum National d'Histoire Naturelle, Paris, France.
3
Department of Chemistry, University of Oxford, Oxford, UK.

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.

PMID:
24705590
PMCID:
PMC3992131
DOI:
10.1038/nchembio.1499
[Indexed for MEDLINE]
Free PMC Article

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