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

SASDLJ9 – Menangle virus (MenV) phosphoprotein C-terminal fragment, amino acids 267-328 (flexible linker)

Phosphoprotein
MWexperimental 6 kDa
MWexpected 6 kDa
VPorod 12 nm3
log I(s) 1.99×10-2 1.99×10-3 1.99×10-4 1.99×10-5
Phosphoprotein small angle scattering data  s, nm-1
ln I(s)
Phosphoprotein Guinier plot ln 2.00×10-2 Rg: 2.5 nm 0 (2.5 nm)-2 s2
(sRg)2I(s)/I(0)
Phosphoprotein Kratky plot 1.104 0 3 sRg
p(r)
Phosphoprotein pair distance distribution function Rg: 2.6 nm 0 Dmax: 10.3 nm

Data validation


There are no models related to this curve.

Synchrotron SAXS data from solutions of MenV phosphoprotein, amino acids 267-328 in 12.5 mM Tris/HCl pH 8.5, 150 mM NaCl, pH 8.5 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 3.62 mg/ml was measured at 20°C. 35 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 L)
Mol. type   Protein
Organism   Menangle virus
Olig. state   Monomer
Mon. MW   6.5 kDa
 
UniProt   Q91MK1 (267-328)
Sequence   FASTA