Phosphorylation toggles the SARS-CoV-2 nucleocapsid protein between two membrane-associated condensate states.

Favetta B Wang H, Cubuk J, Singh A, Barai M, Ramirez C, Zheng H, Gormley AJ, Murthy NS, Dignon G, Soranno A, Shi Z, Schuster BS, Nat Commun 16(1):7970 (2025) Europe PMC

SASDX86 – Phosphorylated SARS-CoV-2 Nucleocapsid protein 3 mg/mL

Nucleoprotein
MWexperimental 96 kDa
MWexpected 95 kDa
log I(s) 1.09×101 1.09×100 1.09×10-1 1.09×10-2
Nucleoprotein small angle scattering data  s, nm-1
ln I(s)
Nucleoprotein Guinier plot ln 1.09×101 Rg: 5.9 nm 0 (5.9 nm)-2 s2
(sRg)2I(s)/I(0)
Nucleoprotein Kratky plot 1.104 0 √3 sRg
Dmax: 19.8 nm

Data validation

There are no models related to this curve.

Synchrotron SAXS data from solutions of SARS-CoV-2 Phosphorylated SARS-Cov-2 Nucleocapsid protein in 20 mM Tris, 150 mM NaCl, pH 7.5 were collected on the 16-ID (LiX) beam line at the National Synchrotron Light Source II (NSLS-II) storage ring (Upton, NY, USA) of λ = 0.08189 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). Phosphorylation was carried out in vitro using GSK3b and SRPK1 kinases.SAXS data was collected over a s range of 0.05 - 31.3 nm-1 and analyzed within a range of 0.05 - 2.55 nm-1. Sample to detector distance for small angles was 3.560 m and 0.317 m for wide angles using Pilatus3X 1M and Pilatus3X 900k detectors. One solute concentration of 3.0 mg/ml was measured at 25°C. 10 successive 0.500 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.

Nucleoprotein
Mol. type   Protein
Organism   Severe acute respiratory syndrome coronavirus 2
Olig. state   Dimer
Mon. MW   47.3 kDa
 
UniProt   P0DTC9 (2-419)
Sequence   FASTA