4ZGV

The Crystal Structure of the Ferredoxin Receptor FusA from Pectobacterium atrosepticum SCRI1043

Summary for 4ZGV

• Entry DOI: 10.2210/pdb4zgv/pdb
• Descriptor: Ferredoxin receptor, LAURYL DIMETHYLAMINE-N-OXIDE, octyl beta-D-glucopyranoside, ... (4 entities in total)
• Functional Keywords: beta-barrel, tonb-dependent receptor, iron-transporter, outer membrane, transport protein
• Biological source: Pectobacterium atrosepticum
• Total number of polymer chains: 2
• Total formula weight: 197201.40

Authors

Grinter, R.,Josts, I.,Roszak, A.W.,Cogdell, R.J.,Walker, D. (deposition date: 2015-04-24, release date: 2016-08-31, Last modification date: 2024-10-09)

Primary citation

Grinter, R.,Josts, I.,Mosbahi, K.,Roszak, A.W.,Cogdell, R.J.,Bonvin, A.M.,Milner, J.J.,Kelly, S.M.,Byron, O.,Smith, B.O.,Walker, D.
Structure of the bacterial plant-ferredoxin receptor FusA.
Nat Commun, 7:13308-13308, 2016

PubMed 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.

PubMed: 27796364
DOI: 10.1038/ncomms13308

Experimental method

X-RAY DIFFRACTION (3.2 Å)