Structure and stability of the Human respiratory syncytial virus M2-1 RNA-binding core domain reveals a compact and cooperative folding unit.

Molina IG, Josts I, Almeida Hernandez Y, Esperante S, Salgueiro M, Garcia Alai MM, de Prat-Gay G, Tidow H, Acta Crystallogr F Struct Biol Commun 74(Pt 1):23-30 (2018) Europe PMC

SASDDE3 – Human respiratory syncytial virus (HRSV) M2–1 RNA-binding core domain

Human respiratory syncytial virus M2-1
MWexperimental 15 kDa
MWexpected 14 kDa
VPorod 3 nm3
log I(s) 3.82×103 3.82×102 3.82×101 3.82×100
Human respiratory syncytial virus M2-1 small angle scattering data  s, nm-1
ln I(s)
Human respiratory syncytial virus M2-1 Guinier plot ln 3.83×103 Rg: 2.0 nm 0 (2.0 nm)-2 s2
(sRg)2I(s)/I(0)
Human respiratory syncytial virus M2-1 Kratky plot 1.104 0 √3 sRg
p(r)
Human respiratory syncytial virus M2-1 pair distance distribution function Rg: 2.1 nm 0 Dmax: 7.9 nm

Data validation

Fits and models

log I(s)
 s, nm-1
Human respiratory syncytial virus M2-1 DAMMIF model
Synchrotron SAXS data from solutions of Human respiratory syncytial virus (HRSV) M 2–1 RNA-binding core domain in 20 mM Tris-HCl, 300 mM NaCl, pH 7, were collected on the EMBL-P12 beam line at the PETRA III storage ring (DESY, Hamburg, Germany) using a Pilatus 2M detector at a sample-detector distance of 3 m and at a wavelength of λ = 0.124 nm (l(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). Solute concentrations ranging between 4.5 and 9 mg/ml were measured at 10°C. 20 successive 0.045 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.

Human respiratory syncytial virus M2-1 (HRSV M2-1)
Mol. type   Protein
Organism   Human orthopneumovirus
Olig. state   Monomer
Mon. MW   13.7 kDa
 
UniProt   Q4KRW3 (73-194)
Sequence   FASTA