Disulfide isomerase activity of the dynamic, trimeric Proteus mirabilis ScsC protein is primed by the tandem immunoglobulin-fold domain of ScsB.

Furlong EJ, Choudhury HG, Kurth F, Duff AP, Whitten AE, Martin JL, J Biol Chem 293(16):5793-5805 (2018) Europe PMC

SASDC48 – ScsC-ScsBalpha complex

DsbA-like protein
Putative metal resistance protein
MWI(0) 95 kDa
MWexpected 105 kDa
VPorod 145 nm3
log I(s) 4.05×10-2 4.05×10-3 4.05×10-4 4.05×10-5
DsbA-like protein Putative metal resistance protein small angle scattering data  s, nm-1
ln I(s)
DsbA-like protein Putative metal resistance protein Guinier plot ln 4.06×10-2 Rg: 3.9 nm 0 (3.9 nm)-2 s2
(sRg)2I(s)/I(0)
DsbA-like protein Putative metal resistance protein Kratky plot 1.104 0 √3 sRg
p(r)
DsbA-like protein Putative metal resistance protein pair distance distribution function Rg: 3.9 nm 0 Dmax: 11.5 nm

Data validation

Fits and models

log I(s)
 s, nm-1
DsbA-like protein Putative metal resistance protein SASREF model
X-ray synchrotron radiation scattering data from solutions of Suppressor of Copper Sensitivity C protein (ScsC) complexed with the alpha domain of the Suppressor of Copper Sensitivity B protein from Proteus mirabilis in 10 mM HEPES 100mM NaCl, pH 7.5 were collected on the SAXS/WAXS beam line of the Australian Synchrotron (Melbourne, Australia) using a 2D Photon counting Pilatus 1M-W pixel detector (s = 4π sin θ/λ, where 2θ is the scattering angle). Thirteen successive 1 second frames were collected across solute concentrations of 0.56-4.50 mg/ml. The SAXS data displayed this entry was derived from a 0.56 mg/ml sample. The data were normalized to the intensity of the transmitted beam and radially averaged and the scattering of the solvent-blank was subtracted. Small-angle neutron scattering data with contrast variation were also collected on the QUOKKA instrument at the Australian Nuclear Science and Technology Organisation at a solute concentration of ~5.0 mg/ml. A rigid-body model was co-refined against the SAXS and SANS data using using SASREF (v 7.d), and this model is shown, together with the X-ray data and correspond fit. Details of the SANS data collection, corresponding fits, and additional analysis are contained in a downloadable zip archive.

DsbA-like protein (ScsC)
Mol. type   Protein
Organism   Proteus mirabilis
Olig. state   Trimer
Mon. MW   24.8 kDa
 
UniProt   C2LPE2 (22-243)
Sequence   FASTA
 
Putative metal resistance protein (ScsB)
Mol. type   Protein
Organism   Proteus mirabilis
Olig. state   Monomer
Mon. MW   30.3 kDa
 
UniProt   B4EV20 (22-275)
Sequence   FASTA