A Structural and Dynamic Analysis of the Partially Disordered Polymerase-Binding Domain in RSV Phosphoprotein

Cardone C, Caseau C, Bardiaux B, Thureaux A, Galloux M, Bajorek M, Eléouët J, Litaudon M, Bontems F, Sizun C, Biomolecules 11(8):1225 (2021) DOI

SASDJD2 – Human respiratory syncytial virus A (RSV) phosphoprotein oligomerization domain

Phosphoprotein
MWexperimental 32 kDa
MWexpected 18 kDa
VPorod 33 nm3
log I(s) 4.47×10-2 4.47×10-3 4.47×10-4 4.47×10-5
Phosphoprotein small angle scattering data  s, nm-1
ln I(s)
Phosphoprotein Guinier plot ln 4.48×10-2 Rg: 2.1 nm 0 (2.1 nm)-2 s2
(sRg)2I(s)/I(0)
Phosphoprotein Kratky plot 1.104 0 √3 sRg
p(r)
Phosphoprotein pair distance distribution function Rg: 2.2 nm 0 Dmax: 7.6 nm

Data validation

Fits and models

log I(s)
 s, nm-1
Phosphoprotein MULTIFOXS model
Synchrotron SAXS data from solutions of Human respiratory syncytial virus A (RSV) phosphoprotein oligomerization domain in 20 mM Na phosphate 100 mM NaCl, pH 6.5 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 2 m and at a wavelength of λ = 0.103 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). One solute concentration of 1.10 mg/ml was measured at 20°C. 10 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.

Phosphoprotein
Mol. type   Protein
Organism   Respiratory syncytial virus
Olig. state   Tetramer
Mon. MW   4.6 kDa
 
UniProt   P12579 (127-163)
Sequence   FASTA