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Structure of the bacterial plant-ferredoxin receptor FusA

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  • Rhys Grinter

    (Institute of Infection, Immunity and Inflammation, College of Medical, Veterinary and Life Sciences, University of Glasgow
    Institute of Microbiology and Infection, School of Immunity and Infection, University of Birmingham
    Infection and Immunity Program, Monash University)

  • Inokentijs Josts

    (Institute of Infection, Immunity and Inflammation, College of Medical, Veterinary and Life Sciences, University of Glasgow)

  • Khedidja Mosbahi

    (Institute of Infection, Immunity and Inflammation, College of Medical, Veterinary and Life Sciences, University of Glasgow)

  • Aleksander W. Roszak

    (Institute of Molecular, Cell and Systems Biology, College of Medical, Veterinary and Life Sciences, 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)

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.

Suggested Citation

  • Rhys Grinter & Inokentijs Josts & Khedidja Mosbahi & Aleksander W. Roszak & Richard J. Cogdell & Alexandre M. J. J. Bonvin & Joel J. Milner & Sharon M. Kelly & Olwyn Byron & Brian O. Smith & Daniel Wa, 2016. "Structure of the bacterial plant-ferredoxin receptor FusA," Nature Communications, Nature, vol. 7(1), pages 1-10, December.
  • Handle: RePEc:nat:natcom:v:7:y:2016:i:1:d:10.1038_ncomms13308
    DOI: 10.1038/ncomms13308
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    Cited by:

    1. Rhys Grinter & Iain D Hay & Jiangning Song & Jiawei Wang & Don Teng & Vijay Dhanesakaran & Jonathan J Wilksch & Mark R Davies & Dene Littler & Simone A Beckham & Ian R Henderson & Richard A Strugnell , 2018. "FusC, a member of the M16 protease family acquired by bacteria for iron piracy against plants," PLOS Biology, Public Library of Science, vol. 16(8), pages 1-21, August.

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