Engineered variants provide new insight into the structural properties important for activity of the highly dynamic, trimeric protein disulfide isomerase ScsC from Proteus mirabilis.

Furlong EJ, Kurth F, Premkumar L, Whitten AE, Martin JL, Acta Crystallogr D Struct Biol 75(Pt 3):296-307 (2019) Europe PMC

SASDER4 – Wild-type suppressor of copper sensitivity C protein, PmScsC, with concentration series data

Suppressor of Copper Sensitivity C protein
MWexperimental 83 kDa
MWexpected 74 kDa
VPorod 101 nm3
log I(s) 4.10×10-1 4.10×10-2 4.10×10-3 4.10×10-4
Suppressor of Copper Sensitivity C protein small angle scattering data  s, nm-1
ln I(s)
Suppressor of Copper Sensitivity C protein Guinier plot ln 4.10×10-1 Rg: 3.7 nm 0 (3.7 nm)-2 s2
(sRg)2I(s)/I(0)
Suppressor of Copper Sensitivity C protein Kratky plot 1.104 0 √3 sRg
p(r)
Suppressor of Copper Sensitivity C protein pair distance distribution function Rg: 3.6 nm 0 Dmax: 11.1 nm

Data validation

Fits and models

log I(s)
 s, nm-1
Suppressor of Copper Sensitivity C protein OTHER model
X-ray synchrotron radiation scattering data from solutions of Suppressor of Copper Sensitivity C protein (ScsC) protein from Proteus mirabilis in 10 mM HEPES 150mM NaCl, pH 7.4 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). Thirty eight successive 1 second frames were collected across solute concentrations of 0.1-10.0 mg/ml at a sample temperature of 10°C. The data were normalized to the intensity of the transmitted beam and radially averaged and the scattering of the solvent-blank was subtracted. The SAXS data displayed this entry was derived from a 10.0 mg/ml sample and show that essentially only trimer is present in solution. A linear combination of monomer and trimer are fit to the scattering curve, and the final concentration of each species in solution was determined to be: 0.08 µM (monomer); 95.05 µM (trimer). Together, with data collected at other concentration (available to download as a zip archive), it was estimated that K1 (3monomer <-> trimer) was 6.3 nM^2.

Suppressor of Copper Sensitivity C protein (PmScsC)
Mol. type   Protein
Organism   Proteus mirabilis
Olig. state   Trimer
Mon. MW   24.8 kDa
 
UniProt   A0A1Z1SYD5 (22-243)
Sequence   FASTA
 
PDB ID   6MHH