Structure of the aminoterminal domain of the birnaviral multifunctional VP3 protein and its unexplored critical role.

Ferrero DS Gimenez MC, Sagar A, Rodríguez JM, Castón JR, Terebiznik MR, Bernadó P, Verdaguer N, PNAS Nexus 3(12):pgae521 (2024) Europe PMC

SASDUS7 – Infectious Bursal Disease Virus VP3 (C-terminal deleted at pH 8.0)

Structural polyprotein (Capsid protein VP3: K947R; Δ977-1012)
MWexperimental 56 kDa
MWexpected 55 kDa
VPorod 110 nm3
log I(s) 5.50×10-2 5.50×10-3 5.50×10-4 5.50×10-5
Structural polyprotein (Capsid protein VP3: K947R; Δ977-1012) small angle scattering data  s, nm-1
ln I(s)
Structural polyprotein (Capsid protein VP3: K947R; Δ977-1012) Guinier plot ln 5.50×10-2 Rg: 4.1 nm 0 (4.1 nm)-2 s2
(sRg)2I(s)/I(0)
Structural polyprotein (Capsid protein VP3: K947R; Δ977-1012) Kratky plot 1.104 0 √3 sRg
Dmax: 15 nm

Data validation

There are no models related to this curve.

Synchrotron SAXS data from solutions of Infectious Bursal Disease Virus VP3 (C-terminal deleted) in 50 mM TRIS, 500 mM NaCl, 2 mM DTT, pH 8 were collected on the EMBL P12 beam line at PETRA III (DESY; Hamburg, Germany) using a Pilatus 6M detector at a sample-detector distance of 3 m and at a wavelength of λ = 0.124 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). One solute concentration of 1.09 mg/ml was measured. 40 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

Cell temperature = UNKNOWN. Storage temperature = UNKNOWN

Structural polyprotein (Capsid protein VP3: K947R; Δ977-1012) (IBDV VP3)
Mol. type   Protein
Organism   Infectious bursal disease virus
Olig. state   Dimer
Mon. MW   27.6 kDa
 
UniProt   P61825 (756-976)
Sequence   FASTA