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

SASDDU6 – The ferredoxin protease, FusC, E83A mutant

Ferredoxin protease E83A mutant
MWexperimental 100 kDa
MWexpected 101 kDa
VPorod 152 nm3
log I(s) 2.80×10-1 2.80×10-2 2.80×10-3 2.80×10-4
Ferredoxin protease E83A mutant small angle scattering data  s, nm-1
ln I(s)
Ferredoxin protease E83A mutant 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 Kratky plot 1.104 0 √3 sRg
p(r)
Ferredoxin protease E83A mutant pair distance distribution function Rg: 3.7 nm 0 Dmax: 13.8 nm

Data validation

There are no models related to this curve.

Synchrotron SAXS data from solutions of ferredoxin protease, FusC, E83A mutant 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 = 1.03 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.

FusC E83A mutant at 30 uM (in the absence of Arabidopsis ferredoxin).

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