Structural basis for hijacking siderophore receptors by antimicrobial lasso peptides

DOI: 10.1038/nchembio.1499
PMID: 24705590

Authors: Indran Mathavan (Imperial College London) , Séverine Zirah (UMR 7245 CNRS-Muséum National d'Histoire Naturelle) , Shahid Mehmood (University of Oxford) , Hassan Choudhury (Imperial College London) , Christophe Goulard (UMR 7245 CNRS-Muséum National d'Histoire Naturelle) , Yanyan Li (UMR 7245 CNRS-Muséum National d'Histoire Naturelle) , Carol V Robinson (University of Oxford) , Sylvie Rebuffat (UMR 7245 CNRS-Muséum National d'Histoire Naturelle) , 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

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

Diamond Keywords: Bacteria

Subject Areas: Biology and Bio-materials, Chemistry, Medicine


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

Added On: 29/05/2014 09:14

Discipline Tags:

Antibiotic Resistance Health & Wellbeing Biochemistry Chemistry Structural biology Drug Discovery Life Sciences & Biotech

Technical Tags:

Diffraction Macromolecular Crystallography (MX)