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Structural basis for hijacking siderophore receptors by antimicrobial lasso peptides

DOI: 10.1038/nchembio.1499 DOI Help
PMID: 24705590 PMID Help

Authors: Indran Mathavan (Imperial College London) , Séverine Zirah (Communication Molecules and Adaptation of Microorganisms Laboratory, UMR 7245 CNRS–Muséum National d'Histoire Naturelle, Paris) , Shahid Mehmood (Department of Chemistry, University of Oxford) , Hassan Choudhury (Imperial College London) , Christophe Goulard (Communication Molecules and Adaptation of Microorganisms Laboratory, UMR 7245 CNRS–Muséum National d'Histoire Naturelle, Paris) , Yanyan Li (Communication Molecules and Adaptation of Microorganisms Laboratory, UMR 7245 CNRS–Muséum National d'Histoire Naturelle, Paris) , Carol V Robinson (Department of Chemistry, University of Oxford) , Sylvie Rebuffat (Communication Molecules and Adaptation of Microorganisms Laboratory, UMR 7245 CNRS–Muséum National d'Histoire Naturelle, Paris) , Konstantinos Beis (Diamond Light Source)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Nature Chemical Biology , VOL 10 (5) , PAGES 340 - 342

State: Published (Approved)
Published: April 2014

Open Access Open Access

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.

Journal Keywords: Bacterial; Bacteriocins; Endocytosis; Escherichia; Models; Molecular; Protein; Receptors; Cell Surface

Subject Areas: Biology and Bio-materials, Chemistry


Instruments: I04-1-Macromolecular Crystallography (fixed wavelength)

Added On: 29/05/2014 09:14

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