Structure of the bacterial plant-ferredoxin receptor FusA

Grinter, R. et al. (2016) Structure of the bacterial plant-ferredoxin receptor FusA. Nature Communications, 7, 13308. (doi:10.1038/ncomms13308) (PMID:27796364) (PMCID:PMC5095587)

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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.

Item Type:Articles
Status:Published
Refereed:Yes
Glasgow Author(s) Enlighten ID:Walker, Professor Daniel and Cogdell, Professor Richard and Kelly, Dr Sharon and Milner, Dr Joel and Grinter, Mr Rhys and Smith, Dr Brian and Roszak, Dr Aleksander and Byron, Professor Olwyn and Mosbahi, Dr Khedidja
Authors: Grinter, R., Josts, I., Mosbahi, K., Roszak, A. W., Cogdell, R. J., Bonvin, A. M.J.J., Milner, J. J., Kelly, S. M., Byron, O., Smith, B. O., and Walker, D.
College/School:College of Medical Veterinary and Life Sciences > Institute of Infection Immunity and Inflammation
College of Medical Veterinary and Life Sciences > Institute of Molecular Cell and Systems Biology
Journal Name:Nature Communications
Publisher:Nature Publishing Group
ISSN:2041-1723
Copyright Holders:Copyright © 2016 The Authors
First Published:First published in Nature Communications 7:13308
Publisher Policy:Reproduced under a Creative Commons License

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Project CodeAward NoProject NamePrincipal InvestigatorFunder's NameFunder RefLead Dept
650711A novel mechanism of protein uptake in Gram-negative bacteriaDaniel WalkerBiotechnology and Biological Sciences Research Council (BBSRC)BB/L02022X/1III - BACTERIOLOGY
558551Development of pyocins active against Pseudomonas aeruginosaDaniel WalkerWellcome Trust (WELLCOME)093592/Z/10/ZIII - BACTERIOLOGY
558553Development of pyocins active against Pseudomonas aeruginosaDaniel WalkerWellcome Trust (WELLCOME)093592/Z/10/ZIII - BACTERIOLOGY