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

SASDDQ6 – The ferredoxin protease, FusC

Ferredoxin Protease
MWexperimental 100 kDa
MWexpected 101 kDa
VPorod 152 nm3
log I(s) 1.30×10-1 1.30×10-2 1.30×10-3 1.30×10-4
Ferredoxin Protease small angle scattering data  s, nm-1
ln I(s)
Ferredoxin Protease Guinier plot ln 1.30×10-1 Rg: 3.7 nm 0 (3.7 nm)-2 s2
Ferredoxin Protease Kratky plot 1.104 0 3 sRg
Ferredoxin Protease pair distance distribution function Rg: 3.7 nm 0 Dmax: 12.8 nm

Data validation

There are no models related to this curve.

Synchrotron SAXS data, I(s) vs s (s = 4π sin θ/λ, where 2θ is the scattering angle) were collected from a sample of ferredoxin protease, FusC, using continuous-flow size-exclusion chromatography SAXS (SEC-SAXS) at the SAXS/WAXS beam line at the Australian Synchrotron (Melbourne, Australia). Data were collected a using a Pilatus 1M detector at a sample-detector distance of 2.7 m and at a wavelength of λ = 0.103 nm. The SEC mobile phase consisted of 20 mM Tris, 150 mM NaCl, 0.03 % NaN3, 5.0 % v/v glycerol, pH 7.8, (20°C). The SAXS data data measured from the SEC-elution (sample peak and buffer) were normalized to the intensity of the transmitted beam and radially averaged. The data from the sample SEC-peak were scaled and averaged and the scattering of the solvent-blank was subtracted from the sample frames to produce the data displayed in this entry.

Additional SEC parameters: Column type: GE Healthcare Superdex S200 10/300; Flow rate: 0.4 ml/min; Sample injection concentration: 10 mg/ml; Injection volume: 100 µl.

Ferredoxin Protease (FusC)
Mol. type   Protein
Organism   Pectobacterium atrosepticum SCRI1043
Olig. state   Monomer
Mon. MW   101.3 kDa
UniProt   Q6D8U3 (26-924)
Sequence   FASTA