Structural insights into the multifunctionality of rabies virus P3 protein.

Sethi A, Rawlinson SM, Dubey A, Ang CS, Choi YH, Yan F, Okada K, Rozario AM, Brice AM, Ito N, Williamson NA, Hatters DM, Bell TDM, Arthanari H, Moseley GW, Gooley PR, Proc Natl Acad Sci U S A 120(14):e2217066120 (2023) Europe PMC

SASDQH4 – Attenuated Nishigahara Phosphoprotein Isoform 3 (Ni-CE P3)

Attenuated derivative P3 of Phosphoprotein
MWexperimental 57 kDa
MWexpected 55 kDa
VPorod 127 nm3
log I(s) 3.97×10-3 3.97×10-4 3.97×10-5 3.97×10-6
Attenuated derivative P3 of Phosphoprotein small angle scattering data  s, nm-1
ln I(s)
Attenuated derivative P3 of Phosphoprotein Guinier plot ln 3.98×10-3 Rg: 4.0 nm 0 (4.0 nm)-2 s2
(sRg)2I(s)/I(0)
Attenuated derivative P3 of Phosphoprotein Kratky plot 1.104 0 √3 sRg
Dmax: 17.5 nm

Data validation

Fits and models

log I(s)
 s, nm-1
Attenuated Nishigahara Phosphoprotein Isoform 3 (Ni-CE P3) Rg histogram Rg, nm
Attenuated derivative P3 of Phosphoprotein EOM/RANCH model
Attenuated derivative P3 of Phosphoprotein EOM/RANCH model
Attenuated derivative P3 of Phosphoprotein EOM/RANCH model
Attenuated derivative P3 of Phosphoprotein EOM/RANCH model
Synchrotron SAXS data from solutions of Attenuated Nishigahara Phosphoprotein Isoform 3 (Ni-CE P3) in 25 mM HEPES, 150 mM NaCl, 1 mM TCEP, pH 7.4 were collected on the SAXS/WAXS beam line at the Australian Synchrotron storage ring (Melbourne, Australia) using a Pilatus3 S 2M detector at a sample-detector distance of 3.3 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 5.00 mg/ml was measured at 22°C. One 1 second frame was collected. The data were normalized to the intensity of the transmitted beam and radially averaged; the scattering of the solvent-blank was subtracted.

Attenuated derivative P3 of Phosphoprotein (Ni-CE P3)
Mol. type   Protein
Olig. state   Dimer
Mon. MW   27.5 kDa
Sequence   FASTA