A fold switch regulates conformation of an alphavirus RNA-dependent RNA polymerase.

Arnold JJ, Braet SM, Vieira LC, Moustafa IM, Gohara DW, Fecko JA, Su YN, Jain A, Aponte-Diaz D, Wilke CO, Anand GS, Yennawar NH, Cameron CE, Nucleic Acids Res 54(2) (2026) Europe PMC

SASDXC9 – O'Nyong Nyong virus C-terminus-50residues-nsP3-nsP4 fusion protein

50-residue-C-terminus-nsP3 fused with RNA-directed RNA polymerase nsP4
MWexperimental 318 kDa
MWexpected 318 kDa
log I(s) 1.62×101 1.62×100 1.62×10-1 1.62×10-2
50-residue-C-terminus-nsP3 fused with RNA-directed RNA polymerase nsP4 small angle scattering data  s, nm-1
ln I(s)
50-residue-C-terminus-nsP3 fused with RNA-directed RNA polymerase nsP4 Guinier plot ln 1.62×101 Rg: 5.2 nm 0 (5.2 nm)-2 s2
(sRg)2I(s)/I(0)
50-residue-C-terminus-nsP3 fused with RNA-directed RNA polymerase nsP4 Kratky plot 1.104 0 √3 sRg

Data validation

There are no models related to this curve.

SAXS data from solutions of O'Nyong Nyong virus C-terminus-50residues-nsP3-nsP4 fusion protein in 25 mM HEPES 5% glycerol, 1 mM TCEP, 500 mM NaCl., pH 7.5 were collected on the Rigaku BioSAXS-2000 instrument (Pennsylvania State University, University Park, PA, USA) using a Rigaku HyPix-3000 detector at a sample-detector distance of 0.5 m and at a wavelength of λ = 0.154 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). One solute concentration of 1.80 mg/ml was measured at 4°C. Six successive 600 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.

50-residue-C-terminus-nsP3 fused with RNA-directed RNA polymerase nsP4 (50Cter-nsP3-nsP4)
Mol. type   Protein
Organism   O'nyong nyong virus
Olig. state   Tetramer
Mon. MW   74.9 kDa
 
UniProt   O90368 (1853-2513)
Sequence   FASTA