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
(sRg)2I(s)/I(0)
Ferredoxin Protease Kratky plot 1.104 0 √3 sRg
p(r)
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