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)

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 Milner, Dr Joel and Smith, Dr Brian and Byron, Professor Olwyn and Cogdell, Professor Richard and Grinter, Mr Rhys and Mosbahi, Dr Khedidja and Kelly, Dr Sharon and Roszak, Dr Aleksander
• 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 > School of Infection & Immunity; College of Medical Veterinary and Life Sciences > School of Molecular Biosciences
• Journal Name: Nature Communications
• Publisher: Nature Research
• 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

Project Code	Award No	Project Name	Principal Investigator	Funder's Name	Funder Ref	Lead Dept
65071	1	A novel mechanism of protein uptake in Gram-negative bacteria	Daniel Walker	Biotechnology and Biological Sciences Research Council (BBSRC)	BB/L02022X/1	III - BACTERIOLOGY
55855	1	Development of pyocins active against Pseudomonas aeruginosa	Daniel Walker	Wellcome Trust (WELLCOME)	093592/Z/10/Z	III - BACTERIOLOGY
55855	3	Development of pyocins active against Pseudomonas aeruginosa	Daniel Walker	Wellcome Trust (WELLCOME)	093592/Z/10/Z	III - BACTERIOLOGY