Toxin:antitoxin ratio sensing autoregulation of the Vibrio cholerae parDE2 module.

Garcia-Rodriguez G, Girardin Y, Kumar Singh R, Volkov AN, Van Dyck J, Muruganandam G, Sobott F, Charlier D, Loris R, Sci Adv 10(1):eadj2403 (2024) Europe PMC

SASDPN3 – Vibrio cholerae ParD2:ParE2 antitoxin:toxin complex

Antitoxin ParD
Toxin

MW^experimental	78	kDa
MW^expected	79	kDa
V^Porod	140	nm³

log I(s) 4.36×10¹ 4.36×10⁰ 4.36×10^-1 4.36×10^-2

Antitoxin ParD Toxin small angle scattering data

s, nm^-1

Log plot Log-Log plot

ln I(s)

ln 4.37×10¹ R_g: 3.0 nm 0 (3.0 nm)^-2 s²

(sR_g)²I(s)/I(0)

1.104 0 √3 sR_g

D_max: 11 nm

Data validation

Fits and models

log I(s)	s, nm^-1
+3 Δ/σ -3	s, nm^-1

Antitoxin ParD Toxin CUSTOM IN-HOUSE model

Synchrotron SAXS data from solutions of Vibrio cholerae ParD2:ParE2 antitoxin:toxin complex in 20 mM Tris, 150 mM NaCl, 1 mM TCEP, pH 8 were collected on the BM29 beam line at the ESRF (Grenoble, France) using a Pilatus 1M detector at a wavelength of λ = 0.099 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 25.00 μl sample at 18 mg/ml was injected at a 0.20 ml/min flow rate onto a Shodex KW402.5-4F column at 19°C. 2100 successive 1 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.

Sample detector distance = UNKNOWN

Antitoxin ParD (ParD2)
Mol. type		Protein
Organism		Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)
Olig. state		Hexamer
Mon. MW		9.0 kDa

UniProt		P58093 (1-80)
Sequence		FASTA

Toxin (ParE2)
Mol. type		Protein
Organism		Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)
Olig. state		Other
Mon. MW		12.4 kDa

UniProt		Q9KMJ0 (1-99)
Sequence		FASTA

PDB ID		7R5A

PDB ID		7R5A

PDB ID		7R5A

PDB ID		7R5A