Structural Insights of Shigella Translocator IpaB and Its Chaperone IpgC in Solution

Ferrari M, Charova S, Sansonetti P, Mylonas E, Gazi A, Frontiers in Cellular and Infection Microbiology 11 (2021) DOI

SASDKQ9 – Chaperone protein IpgC, symmetric dimer from Shigella flexneri

Chaperone protein IpgC
MWI(0) 37 kDa
MWexpected 39 kDa
VPorod 56 nm3
log I(s) 7.33×101 7.33×100 7.33×10-1 7.33×10-2
Chaperone protein IpgC small angle scattering data  s, nm-1
ln I(s)
Chaperone protein IpgC Guinier plot ln 7.33×101 Rg: 2.7 nm 0 (2.7 nm)-2 s2
(sRg)2I(s)/I(0)
Chaperone protein IpgC Kratky plot 1.104 0 √3 sRg
p(r)
Chaperone protein IpgC pair distance distribution function Rg: 2.7 nm 0 Dmax: 9 nm

Data validation

Fits and models

log I(s)
 s, nm-1
Chaperone protein IpgC CORAL model
Synchrotron SAXS data from solutions of IpgC in 20 mM HEPES, 100 mM NaCl, pH 7.4 were collected on the BM29 beam line at the ESRF (Grenoble, France) using a Pilatus 1M detector at a sample-detector distance of 2.8 m and at a wavelength of λ = 0.09199 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). Solute concentrations ranging between 0.2 and 7.8 mg/ml were measured at 10°C. The data were normalized to the intensity of the transmitted beam and radially averaged; the scattering of the solvent-blank was subtracted. The low angle data collected at lower concentration were merged with the highest concentration high angle data to yield the final composite scattering curve.

Storage temperature = UNKNOWN. X-ray Exposure time = UNKNOWN. Number of frames = UNKNOWN

Chaperone protein IpgC (IpgC)
Mol. type   Protein
Organism   Shigella flexneri
Olig. state   Dimer
Mon. MW   19.6 kDa
 
UniProt   P0A2U4 (2-155)
Sequence   FASTA