Structural Insights into Bacteriophage GIL01 gp7 Inhibition of Host LexA Repressor

Caveney N, Pavlin A, Caballero G, Bahun M, Hodnik V, de Castro L, Fornelos N, Butala M, Strynadka N, Structure (2019) DOI

SASDEB8 – Bacillus thuringiensis LexA repressor (Bt_LexA)

Bacillus thuringiensis LexA repressor
MWexperimental 64 kDa
MWexpected 47 kDa
VPorod 110 nm3
log I(s) 9.40×10-1 9.40×10-2 9.40×10-3 9.40×10-4
Bacillus thuringiensis LexA repressor small angle scattering data  s, nm-1
ln I(s)
Bacillus thuringiensis LexA repressor Guinier plot ln 9.40×10-1 Rg: 3.7 nm 0 (3.7 nm)-2 s2
(sRg)2I(s)/I(0)
Bacillus thuringiensis LexA repressor Kratky plot 1.104 0 3 sRg

Data validation


Fits and models


log I(s)
 s, nm-1
Bacillus thuringiensis LexA repressor CHIMERA model

log I(s)
 s, nm-1
Bacillus thuringiensis LexA repressor CHIMERA model

log I(s)
 s, nm-1
Bacillus thuringiensis LexA repressor CHIMERA model

SAXS data from solutions of Bacillus thuringiensis LexA repressor (Bt_LexA) in 20 mM HEPES, 300 mM NaCl, 10% glycerol, pH 8 were collected on a Rigaku BioSAXS-2000 instrument at the University of British Columbia (Vancouver, Canada) using a Hybrid Pixel Array Detector Rigaku HyOix-3000 detector at a wavelength of λ = 0.154 nm (l(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). Solute concentrations ranging between 5 and 40 mg/ml were measured at 6°C. 12 successive 300 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. The low angle data collected at lower concentration were merged with the highest concentration high angle data to yield the final composite scattering curve.

Bacillus thuringiensis LexA repressor (LexA)
Mol. type   Protein
Organism   Bacillus thuringiensis
Olig. state   Dimer
Mon. MW   23.4 kDa
 
UniProt   A0A2B4EEI3 (1-210)
Sequence   FASTA