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PDBsum entry 4zho
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Electron transport
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PDB id
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4zho
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PDB id:
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| Name: |
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Electron transport
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Title:
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The crystal structure of arabidopsis ferredoxin 2 with 2fe-2s cluster
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Structure:
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Ferredoxin-2, chloroplastic. Chain: a, b. Synonym: atfd2. Engineered: yes
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Source:
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Arabidopsis thaliana. Mouse-ear cress. Organism_taxid: 3702. Gene: fd2, petf, petf1, at1g60950, t7p1.9. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008
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Resolution:
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2.34Å
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R-factor:
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0.198
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R-free:
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0.216
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Authors:
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R.Grinter,I.Josts,A.W.Roszak,R.J.Cogdell,D.Walker
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Key ref:
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R.Grinter
et al.
(2016).
Structure of the bacterial plant-ferredoxin receptor FusA.
Nat Commun,
7,
13308.
PubMed id:
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Date:
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26-Apr-15
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Release date:
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31-Aug-16
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PROCHECK
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Headers
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References
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P16972
(FER2_ARATH) -
Ferredoxin-2, chloroplastic from Arabidopsis thaliana
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Seq:
Struc:
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148 a.a.
97 a.a.*
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Key: |
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PfamA domain |
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Secondary structure |
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CATH domain |
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*
PDB and UniProt seqs differ
at 2 residue positions (black
crosses)
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Nat Commun
7:13308
(2016)
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PubMed id:
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Structure of the bacterial plant-ferredoxin receptor FusA.
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R.Grinter,
I.Josts,
K.Mosbahi,
A.W.Roszak,
R.J.Cogdell,
A.M.Bonvin,
J.J.Milner,
S.M.Kelly,
O.Byron,
B.O.Smith,
D.Walker.
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ABSTRACT
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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.
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