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