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

SASDB94 – Suppressor of Copper Sensitivity C protein (ScsC) from Proteus mirabilis

C-terminal catalytic domain of Suppressor of Copper Sensitivity C protein
MWexperimental 70 kDa
MWexpected 20 kDa
VPorod 92 nm3
log I(s) 1.01×10-1 1.01×10-2 1.01×10-3 1.01×10-4
C-terminal catalytic domain of Suppressor of Copper Sensitivity C protein small angle scattering data  s, nm-1
ln I(s)
C-terminal catalytic domain of Suppressor of Copper Sensitivity C protein Guinier plot ln 1.01×10-1 Rg: 3.7 nm 0 (3.7 nm)-2 s2
(sRg)2I(s)/I(0)
C-terminal catalytic domain of Suppressor of Copper Sensitivity C protein Kratky plot 1.104 0 √3 sRg
p(r)
C-terminal catalytic domain of Suppressor of Copper Sensitivity C protein pair distance distribution function Rg: 3.6 nm 0 Dmax: 10.5 nm

Data validation

Fits and models

log I(s)
 s, nm-1
Suppressor of Copper Sensitivity C protein (ScsC) from Proteus mirabilis Rg histogram Rg, nm
C-terminal catalytic domain of Suppressor of Copper Sensitivity C protein EOM/RANCH model
C-terminal catalytic domain of Suppressor of Copper Sensitivity C protein EOM/RANCH model
C-terminal catalytic domain of Suppressor of Copper Sensitivity C protein EOM/RANCH model
C-terminal catalytic domain of Suppressor of Copper Sensitivity C protein EOM/RANCH model
C-terminal catalytic domain of Suppressor of Copper Sensitivity C protein EOM/RANCH model
C-terminal catalytic domain of Suppressor of Copper Sensitivity C protein EOM/RANCH model
log I(s)
 s, nm-1
C-terminal catalytic domain of Suppressor of Copper Sensitivity C protein CORAL model
X-ray synchrotron radiation scattering data from solutions of Suppressor of Copper Sensitivity C protein (ScsC) from Proteus 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 (s = 4π sin θ/λ, where 2θ is the scattering angle). Fourteen successive 2 second frames were collected across solute concentrations of 2.15-8.85 mg/ml. The SAXS data displayed this entry was derived from a 2.15 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 six 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.

Wavelength = UNKNOWN

C-terminal catalytic domain of Suppressor of Copper Sensitivity C protein (PmScsCΔN)
Mol. type   Protein
Organism   Proteus mirabilis
Olig. state   Monomer
Mon. MW   20.2 kDa
 
UniProt   A0A1Z1SYD5 (64-243)
Sequence   FASTA
 
PDB ID   4XVW