FusC, a member of the M16 protease family acquired by bacteria for iron piracy against plants.

Grinter R Hay ID, Song J, Wang J, Teng D, Dhanesakaran V, Wilksch JJ, Davies MR, Littler D, Beckham SA, Henderson IR, Strugnell RA, Dougan G, Lithgow T, PLoS Biol 16(8):e2006026 (2018) Europe PMC

SASDDW6 – The ferredoxin protease, FusC, E83A mutant + 5 µM Arabidopsis ferredoxin

Ferredoxin protease E83A mutant
Arabidopsis ferredoxin 2
MWexperimental 100 kDa
MWexpected 113 kDa
VPorod 148 nm3
log I(s) 2.80×10-1 2.80×10-2 2.80×10-3 2.80×10-4
Ferredoxin protease E83A mutant Arabidopsis ferredoxin 2 small angle scattering data  s, nm-1
ln I(s)
Ferredoxin protease E83A mutant Arabidopsis ferredoxin 2 Guinier plot ln 2.80×10-1 Rg: 3.7 nm 0 (3.7 nm)-2 s2
(sRg)2I(s)/I(0)
Ferredoxin protease E83A mutant Arabidopsis ferredoxin 2 Kratky plot 1.104 0 √3 sRg
p(r)
Ferredoxin protease E83A mutant Arabidopsis ferredoxin 2 pair distance distribution function Rg: 3.7 nm 0 Dmax: 13.7 nm

Data validation

There are no models related to this curve.

Synchrotron SAXS data from solutions of ferredoxin protease, FusC, E83A mutant + 5 µM Arabidopsis ferredoxin in 20 mM Tris, 150 mM NaCl, pH 7.8 were collected on the SAXS/WAXS beam line at the Australian Synchrotron storage ring (Melbourne, Australia) using a Pilatus 1M detector at a sample-detector distance of 1.3 m and at a wavelength of λ = 0.103 nm (l(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). One solute concentration of 3.00 mg/ml was measured at 20°C. The data were normalized to the intensity of the transmitted beam and radially averaged; the scattering of the solvent-blank was subtracted.

The FusC E83A mutant (30 µM) in the presence of 5 µM Arabidopsis ferredoxin. The background subtraction included 5 µM Arabidopsis ferredoxin in buffer.

Ferredoxin protease E83A mutant (FusC E83A)
Mol. type   Protein
Organism   Pectobacterium atrosepticum SCRI1043
Olig. state   Monomer
Mon. MW   101.2 kDa
 
UniProt   Q6D8U3 (26-924)
Sequence   FASTA
 
Arabidopsis ferredoxin 2 (Ara_Fer2)
Mol. type   Protein
Organism   Arabidopsis thaliana
Olig. state   Monomer
Mon. MW   11.3 kDa
 
UniProt   P16972 (53-145)
Sequence   FASTA