Structural Analysis of the Menangle Virus P Protein Reveals a Soft Boundary between Ordered and Disordered Regions

Webby M, Herr N, Bulloch E, Schmitz M, Keown J, Goldstone D, Kingston R, Viruses 13(9):1737 (2021) DOI

SASDLG9 – Menangle virus (MenV) phosphoprotein, amino acids 209-388 (coiled-coil/flexible linker/binding domain and C352S mutation)

MWexperimental 79 kDa
MWexpected 79 kDa
VPorod 524 nm3
log I(s) 2.75×10-1 2.75×10-2 2.75×10-3 2.75×10-4
Phosphoprotein small angle scattering data  s, nm-1
ln I(s)
Phosphoprotein Guinier plot ln 2.76×10-1 Rg: 6.3 nm 0 (6.3 nm)-2 s2
Phosphoprotein Kratky plot 1.104 0 3 sRg
Phosphoprotein pair distance distribution function Rg: 6.4 nm 0 Dmax: 23.4 nm

Data validation

There are no models related to this curve.

Synchrotron SAXS data from solutions of MenV phosphoprotein, amino acids 209-388 in 12.5 mM MOPS/KOH pH 7.0, 250 mM NaCl, pH 7 were collected on the SAXS/WAXS beam line at the Australian Synchrotron (Melbourne, Australia) using a Pilatus 1M detector at a sample-detector distance of 1.4 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 4.80 mg/ml was measured at 20°C. 25 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.

Phosphoprotein (MenV P CC-L-BD)
Mol. type   Protein
Organism   Menangle virus
Olig. state   Tetramer
Mon. MW   19.7 kDa
UniProt   Q91MK1 (209-388)
Sequence   FASTA