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Structure of the bacterial plant-ferredoxin receptor FusA

DOI: 10.1038/ncomms13308 DOI Help

Authors: Rhys Grinter (University of Glasgow; University of Birmingham; Monash University) , Inokentijs Josts (University of Glasgow) , Khedidja Mosbahi (Institute of Infection, Immunity and Inflammation, College of Medical, Veterinary and Life Sciences, University of Glasgow) , Aleksander W. Roszak (University of Glasgow) , Richard J. Cogdell (Institute of Molecular, Cell and Systems Biology, College of Medical, Veterinary and Life Sciences, University of Glasgow) , Alexandre M. J. J. Bonvin (Bijvoet Center for Biomolecular Research, Faculty of Science, Utrecht University) , Joel J. Milner (School of Life Sciences, College of Medical, Veterinary and Life Sciences, University of Glasgow) , Sharon M. Kelly (Institute of Molecular, Cell and Systems Biology, College of Medical, Veterinary and Life Sciences, University of Glasgow) , Olwyn Byron (School of Life Sciences, College of Medical, Veterinary and Life Sciences, University of Glasgow) , Brian O. Smith (Institute of Molecular, Cell and Systems Biology, College of Medical, Veterinary and Life Sciences, University of Glasgow) , Daniel Walker (Institute of Infection, Immunity and Inflammation, College of Medical, Veterinary and Life Sciences, University of Glasgow)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Nature Communications , VOL 7

State: Published (Approved)
Published: October 2016
Diamond Proposal Number(s): 6638 , 8659

Open Access Open Access

Abstract: Iron is a limiting nutrient in bacterial infection putting it at the centre of an evolutionary arms race between host and pathogen. Gram-negative bacteria utilize TonB-dependent outer membrane receptors to obtain iron during infection. These receptors acquire iron either in concert with soluble iron-scavenging siderophores or through direct interaction and extraction from host proteins. Characterization of these receptors provides invaluable insight into pathogenesis. However, only a subset of virulence-related TonB-dependent receptors have been currently described. Here we report the discovery of FusA, a new class of TonB-dependent receptor, which is utilized by phytopathogenic Pectobacterium spp. to obtain iron from plant ferredoxin. Through the crystal structure of FusA we show that binding of ferredoxin occurs through specialized extracellular loops that form extensive interactions with ferredoxin. The function of FusA and the presence of homologues in clinically important pathogens suggests that small iron-containing proteins represent an iron source for bacterial pathogens. DOI: 10.1038/ncomms13308 OPEN 1

Journal Keywords: Outer membrane bacterial plant-ferredoxin receptor FusA 3.2A structure, two ferredoxin structures, docking experiments

Subject Areas: Biology and Bio-materials, Chemistry


Instruments: I02-Macromolecular Crystallography , I03-Macromolecular Crystallography , I04-1-Macromolecular Crystallography (fixed wavelength) , I04-Macromolecular Crystallography , I24-Microfocus Macromolecular Crystallography

Other Facilities: No

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ncomms13308.pdf