Ensemble description of the intrinsically disordered N-terminal domain of the Nipah virus P/V protein from combined NMR and SAXS.

Schiavina M, Salladini E, Murrali MG, Tria G, Felli IC, Pierattelli R, Longhi S, Sci Rep 10(1):19574 (2020) Europe PMC

SASDJB5 – Nipah virus phosphoprotein, N-terminal amino acids 1-406 (PNT)

Phosphoprotein
MWexperimental 47 kDa
MWexpected 45 kDa
VPorod 210 nm3
log I(s) 6.96×101 6.96×100 6.96×10-1 6.96×10-2
Phosphoprotein small angle scattering data  s, nm-1
ln I(s)
Phosphoprotein Guinier plot ln 6.96×101 Rg: 6.2 nm 0 (6.2 nm)-2 s2
(sRg)2I(s)/I(0)
Phosphoprotein Kratky plot 1.104 0 √3 sRg
Dmax: 23 nm

Data validation

Fits and models

log I(s)
 s, nm-1
Nipah virus phosphoprotein, N-terminal amino acids 1-406 (PNT) Rg histogram Rg, nm
log I(s)
 s, nm-1
Nipah virus phosphoprotein, N-terminal amino acids 1-406 (PNT) Rg histogram Rg, nm
Synchrotron SAXS data from solutions of Nipah virus phosphoprotein (PNT, 1-406) in 20 mM Tris-HCl, 0.3 M NaCl, 5 mM DTT, pH 8 were collected on the BM29 beam line at the ESRF (Grenoble, France) using a Pilatus 1M detector at a sample-detector distance of 2.8 m and at a wavelength of λ = 0.0992 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). One solute concentration of 1.20 mg/ml was measured at 20°C. 10 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.

Tags: idp
Phosphoprotein (Protein P (P/V/C))
Mol. type   Protein
Organism   Nipah henipavirus
Olig. state   Monomer
Mon. MW   45.3 kDa
 
UniProt   Q9IK91 (1-406)
Sequence   FASTA