Oligomerization process of Bcl-2 associated X protein revealed from intermediate structures in solution

Shih O, Yeh Y, Liao K, Sung T, Chiang Y, Jeng U, Phys. Chem. Chem. Phys. 2017 19(11):7947-7954 DOI

SASDC83 – Dimeric apoptosis regulator BAX (Bcl-2 associated X)

Apoptosis regulator BAX (Bcl-2 associated X)
MWexperimental 39.5 kDa
MWexpected 42 kDa
VPorod 85.6 nm3
log I(s) 1.57×10-2 1.57×10-3 1.57×10-4 1.57×10-5
Apoptosis regulator BAX (Bcl-2 associated X) small angle scattering data  s, nm-1
ln I(s)
Apoptosis regulator BAX (Bcl-2 associated X) Guinier plot ln 1.58×10-2 Rg: 3.0 nm 0 (3.0 nm)-2 s2
(sRg)2I(s)/I(0)
Apoptosis regulator BAX (Bcl-2 associated X) Kratky plot 1.104 0 3 sRg
p(r)
Apoptosis regulator BAX (Bcl-2 associated X) pair distance distribution function Rg: 3.0 nm 0 Dmax: 9.5 nm

Experimental data validation


Fits and models


log I(s)
 s, nm-1
Apoptosis regulator BAX (Bcl-2 associated X) CORAL model
Synchrotron SAXS data from solutions of dimeric apoptosis regulator BAX (Bcl-2 associated X) in 20mM sodium phosphate, 100mM NaCl, pH 8 were collected on the 23A beam line at the Taiwan Photon Source (NSRRC, Hsinchu, Taiwan) using a Pilatus 1M-F detector at a sample-detector distance of 3.2 m and at a wavelength of λ = 0.08266 nm (I(s) vs s, where s = 4πsinθ/λ and 2θ is the scattering angle). One solute concentration of 2.00 mg/ml was measured at 15°C. Three successive 30 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 to obtain the SAXS profile displayed in this entry.

Apoptosis regulator BAX (Bcl-2 associated X) (BAX)
Mol. type   Protein
Organism   Homo sapiens
Olig. state   Dimer
Mon. MW   21.2 kDa
 
UniProt   Q07812 (1-192)
Sequence   FASTA