A structural study of the cytoplasmic chaperone effect of 14-3-3 proteins on Ataxin-1.

Leysen S Jane Burnley R, Rodriguez E, Milroy LG, Soini L, Adamski CJ, Nitschke L, Davis R, Obsil T, Brunsveld L, Crabbe T, Yahya Zoghbi H, Ottmann C, Martin Davis J, J Mol Biol :167174 (2021) Europe PMC

SASDL56 – 14-3-3 zeta truncated at C-terminus

14-3-3 protein zeta/delta
MWexperimental 47 kDa
MWexpected 53 kDa
log I(s) 6.38×10-2 6.38×10-3 6.38×10-4 6.38×10-5
14-3-3 protein zeta/delta small angle scattering data  s, nm-1
ln I(s)
14-3-3 protein zeta/delta Guinier plot ln 6.39×10-2 Rg: 2.8 nm 0 (2.8 nm)-2 s2
(sRg)2I(s)/I(0)
14-3-3 protein zeta/delta Kratky plot 1.104 0 √3 sRg
p(r)
14-3-3 protein zeta/delta pair distance distribution function Rg: 2.8 nm 0 Dmax: 7.9 nm

Data validation

There are no models related to this curve.

Synchrotron SAXS data from solutions of 14-3-3 zeta truncated at C-terminus in 20 mM HEPES, 150 mM NaCl, 2 mM DTT, pH 7.5 were collected on the B21 beam line at the Diamond Light Source storage ring (Didcot, UK) using a Pilatus 2M detector at a sample-detector distance of 4.0 m and at a wavelength of λ = 0.099873 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). In-line size-exclusion chromatography (SEC) SAS was employed. The SEC parameters were as follows: A 45.00 μl sample at 11.6 mg/ml was injected onto a Shodex KW400 series column at 25°C. 620 successive 3 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.

Storage temperature = UNKNOWN. Flow rate = UNKNOWN

14-3-3 protein zeta/delta (14-3-3z)
Mol. type   Protein
Organism   Homo sapiens
Olig. state   Dimer
Mon. MW   26.3 kDa
 
UniProt   P63104
Sequence   FASTA