Dissecting Henipavirus W proteins conformational and fibrillation properties: contribution of their N- and C-terminal constituent domains.

Pesce G, Gondelaud F, Ptchelkine D, Bignon C, Fourquet P, Longhi S, FEBS J (2024) Europe PMC

SASDUR3 – C-terminal domain of the W protein (CTDw) of Nipah Virus (NiV)

Protein W
MWexperimental 7 kDa
MWexpected 6 kDa
VPorod 8 nm3
log I(s) 1.15×10-2 1.15×10-3 1.15×10-4 1.15×10-5
Protein W small angle scattering data  s, nm-1
ln I(s)
Protein W Guinier plot ln 1.15×10-2 Rg: 2.1 nm 0 (2.1 nm)-2 s2
(sRg)2I(s)/I(0)
Protein W Kratky plot 1.104 0 √3 sRg
p(r)
Protein W pair distance distribution function Rg: 2.2 nm 0 Dmax: 7.8 nm

Data validation

Fits and models

log I(s)
 s, nm-1
C-terminal domain of the W protein (CTDw) of Nipah Virus (NiV) Rg histogram Rg, nm
Protein W EOM/RANCH model
Protein W EOM/RANCH model
Protein W EOM/RANCH model
Protein W EOM/RANCH model
Protein W EOM/RANCH model
Protein W EOM/RANCH model
Protein W EOM/RANCH model
Protein W EOM/RANCH model
Synchrotron SAXS data from solutions of the C-terminal domain of the W protein of Nipah Virus in 20 mM HEPES, 150 mM NaCl, pH 7.2 were collected on the SWING beam line at SOLEIL (Saint-Aubin, France) using a AVIEX PCCD170170 detector at a sample-detector distance of 2 m and at a wavelength of λ = 0.103324 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 70.00 μl sample at 9 mg/ml was injected at a 0.20 ml/min flow rate onto a Agilent Bio SEC-3, 100 Å column at 20°C. The data were normalized to the intensity of the transmitted beam and radially averaged; the scattering of the solvent-blank was subtracted.

Number of frames = UNKNOWN

Protein W (NiV CTDw)
Mol. type   Protein
Organism   Henipavirus nipahense
Olig. state   Monomer
Mon. MW   6.0 kDa
 
UniProt   P0C1C7 (407-450)
Sequence   FASTA