Structural Basis of Clostridium perfringens Enterotoxin Activation and Oligomerization by Trypsin

Ogbu C, Kapoor S, Vecchio A, Toxins 15(11):637 (2023) DOI

SASDSH9 – SAXS data of Clostridium perfringens enterotoxin

Heat-labile enterotoxin B chain
MWexperimental 38 kDa
MWexpected 36 kDa
VPorod 46 nm3
log I(s) 4.30×10-3 4.30×10-4 4.30×10-5 4.30×10-6
Heat-labile enterotoxin B chain small angle scattering data  s, nm-1
ln I(s)
Heat-labile enterotoxin B chain Guinier plot ln 4.31×10-3 Rg: 2.7 nm 0 (2.7 nm)-2 s2
(sRg)2I(s)/I(0)
Heat-labile enterotoxin B chain Kratky plot 1.104 0 √3 sRg
p(r)
Heat-labile enterotoxin B chain pair distance distribution function Rg: 2.9 nm 0 Dmax: 10.2 nm

Data validation

Fits and models

log I(s)
 s, nm-1
Heat-labile enterotoxin B chain GASBOR model
log I(s)
 s, nm-1
Heat-labile enterotoxin B chain EOM/RANCH model
log I(s)
 s, nm-1
Heat-labile enterotoxin B chain PDB (PROTEIN DATA BANK) model
Synchrotron SAXS data from solutions of Clostridium perfringens enterotoxin in 10 mM HEPES, 100 mM NaCl, 2% glycerol, pH 7.4 were collected on the BioCAT 18ID beam line at the Advanced Photon Source (APS), Argonne National Laboratory (Lemont, IL, USA) using a Pilatus3 X 1M detector at a sample-detector distance of 3.6 m and at a wavelength of λ = 0.1033 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). In-line size-exclusion chromatography (SEC) SAS was employed. The SEC parameters were as follows: A 250.00 μl sample at 7 mg/ml was injected at a 0.60 ml/min flow rate onto a Cytiva Superdex 200 Increase 10/300 column at 22°C. 1384 successive 0.500 second frames were collected through the entire SEC elution. The data were normalized to the intensity of the transmitted beam and radially averaged; the scattering of the solvent-blank was subtracted.

Heat-labile enterotoxin B chain (CpE)
Mol. type   Protein
Organism   Clostridium perfringens
Olig. state   Monomer
Mon. MW   35.9 kDa
 
UniProt   P01558 (1-319)
Sequence   FASTA
 
PDB ID   2XH6