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

SASDBL7 – N-terminal domain of Vaccinia virus A46 protein (1-83)

Protein A46
MWexperimental 39 kDa
MWexpected 40 kDa
VPorod 68 nm3
log I(s) 1.49×101 1.49×100 1.49×10-1 1.49×10-2
Protein A46 small angle scattering data  s, nm-1
ln I(s)
Protein A46 Guinier plot ln 1.49×101 Rg: 2.6 nm 0 (2.6 nm)-2 s2
Protein A46 Kratky plot 1.104 0 3 sRg
Protein A46 pair distance distribution function Rg: 2.7 nm 0 Dmax: 9 nm

Data validation

Fits and models

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 the N-terminal domain of Vaccinia virus A46 protein (1-83) 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 15.5 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 (A46-delta)
Mol. type   Protein
Organism   Vaccinia virus
Olig. state   Tetramer
Mon. MW   10.0 kDa
UniProt   P26672 (1-83)
Sequence   FASTA