Vaccinia Virus Immunomodulator A46: A Lipid and Protein-Binding Scaffold for Sequestering Host TIR-Domain Proteins.

Fedosyuk S, Bezerra GA, Radakovics K, Smith TK, Sammito M, Bobik N, Round A, Ten Eyck LF, Djinović-Carugo K, Usón I, Skern T, PLoS Pathog 12(12):e1006079 (2016) Europe PMC

SASDBK7 – Vaccinia virus A46 protein (full-length)

Protein A46
MWexperimental 114 kDa
MWexpected 112 kDa
VPorod 199 nm3
log I(s) 7.55×101 7.55×100 7.55×10-1 7.55×10-2
Protein A46 small angle scattering data  s, nm-1
ln I(s)
Protein A46 Guinier plot ln 7.55×101 Rg: 4.3 nm 0 (4.3 nm)-2 s2
Protein A46 Kratky plot 1.104 0 3 sRg
Protein A46 pair distance distribution function Rg: 4.3 nm 0 Dmax: 14 nm

Data validation

Fits and models

log I(s)
 s, nm-1
Protein A46 CORAL model

log I(s)
 s, nm-1
Protein A46 CORAL model

Synchrotron SAXS data, I(s) vs s (s = 4π sin θ/λ, where 2θ is the scattering angle) were collected from a sample of full-length Vaccinia virus A46 protein using continuous-flow size-exclusion chromatography SAXS (SEC-SAXS; Superdex 200 10/300 column) at the BM29 beam line on the ESRF storage ring (Grenoble, France). Data were collected using a Pilatus 1M detector at a sample-detector distance of 2.9 m and at a wavelength of λ = 0.09918 nm. The SEC mobile phase consisted of 20 mM Tris-HCl, 10 mM DTT, pH 8.5, (20°C) with a sample injection concentration of 4.4 mg/ml. Data obtained from solute-free eluates and SEC-elution peak were normalized to the intensity of the transmitted beam and radially averaged; the scattering of the solvent-blank was subtracted from the SEC-peak frames to produce the data displayed in this entry.

Storage temperature = UNKNOWN. Number of frames = UNKNOWN

Protein A46 (VACV A46)
Mol. type   Protein
Organism   Vaccinia virus
Olig. state   Tetramer
Mon. MW   28.0 kDa
UniProt   P26672
Sequence   FASTA