Post-translational acylation drives folding and activity of the CyaA bacterial toxin

Corentin Léger.

SASDXG6 – Adenylate Cyclase Toxine CyaA

Adenylate cyclase Toxin
MWexperimental 182 kDa
MWexpected 178 kDa
VPorod 312 nm3
log I(s) 2.41×10-2 2.41×10-3 2.41×10-4 2.41×10-5
Adenylate cyclase Toxin small angle scattering data  s, nm-1
ln I(s)
Adenylate cyclase Toxin Guinier plot ln 2.41×10-2 Rg: 4.7 nm 0 (4.7 nm)-2 s2
(sRg)2I(s)/I(0)
Adenylate cyclase Toxin Kratky plot 1.104 0 √3 sRg
p(r)
Adenylate cyclase Toxin pair distance distribution function Rg: 4.7 nm 0 Dmax: 16.5 nm

Data validation

Fits and models

log I(s)
 s, nm-1
Adenylate cyclase Toxin ALPHAFOLD model
log I(s)
 s, nm-1
Adenylate cyclase Toxin GROMACS model
Synchrotron SAXS data from solutions of Adenylate Cyclase Toxine CyaA in 20mM HEPES , 50mM NaCl, 2mM CaCl2, pH 7.4 were collected on the SWING beam line at the SOLEIL storage ring (Saint-Aubin, France) using a Eiger 4M detector at a sample-detector distance of 4 m and at a wavelength of λ = 0.1033 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). One solute concentration of 2.94 mg/ml was measured at 15°C. 15 successive 0.990 second frames were collected. The data were normalized to the intensity of the transmitted beam and radially averaged; the scattering of the solvent-blank was subtracted.

Adenylate cyclase Toxin (CyaA)
Mol. type   Protein
Organism   Escherichia coli
Olig. state   Monomer
Mon. MW   177.6 kDa
 
UniProt   P0DKX7
Sequence   FASTA