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