A shape-shifting redox foldase contributes to Proteus mirabilis copper resistance.

Furlong EJ, Lo AW, Kurth F, Premkumar L, Totsika M, Achard MES, Halili MA, Heras B, Whitten AE, Choudhury HG, Schembri MA, Martin JL, Nat Commun 8:16065 (2017) Europe PMC

SASDBW6 – Suppressor of Copper Sensitivity C protein (ScsC) from P. mirabilis (mutant)

Suppressor of Copper Sensitivity C protein (mutant)
MWI(0) 76 kDa
MWexpected 73 kDa
VPorod 108 nm3
log I(s) 6.63×10-2 6.63×10-3 6.63×10-4 6.63×10-5
Suppressor of Copper Sensitivity C protein (mutant) small angle scattering data  s, nm-1
ln I(s)
Suppressor of Copper Sensitivity C protein (mutant) Guinier plot ln 6.63×10-2 Rg: 4.4 nm 0 (4.4 nm)-2 s2
(sRg)2I(s)/I(0)
Suppressor of Copper Sensitivity C protein (mutant) Kratky plot 1.104 0 √3 sRg
p(r)
Suppressor of Copper Sensitivity C protein (mutant) pair distance distribution function Rg: 4.4 nm 0 Dmax: 13.5 nm

Data validation

Fits and models

log I(s)
 s, nm-1
Suppressor of Copper Sensitivity C protein (ScsC) from P. mirabilis (mutant) Rg histogram Rg, nm
Suppressor of Copper Sensitivity C protein (mutant) EOM/RANCH model
Suppressor of Copper Sensitivity C protein (mutant) EOM/RANCH model
Suppressor of Copper Sensitivity C protein (mutant) EOM/RANCH model
Suppressor of Copper Sensitivity C protein (mutant) EOM/RANCH model
log I(s)
 s, nm-1
Suppressor of Copper Sensitivity C protein (mutant) CORAL model
X-ray synchrotron radiation scattering data from solutions of a Suppressor of Copper Sensitivity C mutant protein (ScsC) from P. mirabilis in 25 mM HEPES 150mM NaCl, 1mM DTT, 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 (I(s) vs s, where s = 4π sin θ/λ and 2θ is the scattering angle). Twenty three successive 1 second frames were collected across solute concentrations of 0.60-5.30 mg/ml. The SAXS data displayed this entry was derived from a 1.30 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. The models and corresponding fits include those derived from rigid-body modelling using CORAL (top) and a representative ensemble of four trimeric ScsC structures determined using ensemble optimization method (EOM). The Rg and Dmax distributions derived from EOM are included in the full entry zip archive.

Suppressor of Copper Sensitivity C protein (mutant) (PmScsC (DsbA-like))
Mol. type   Protein
Organism   Proteus mirabilis
Olig. state   Trimer
Mon. MW   24.3 kDa
 
UniProt   C2LPE2 (22-243)
Sequence   FASTA
 
PDB ID   4XVW