14-3-3 protein inhibits CaMKK1 by blocking the kinase active site with its last two C-terminal helices.

Petrvalska O, Honzejkova K, Koupilova N, Herman P, Obsilova V, Obsil T, Protein Sci :e4805 (2023) Europe PMC

SASDSJ7 – Human C-terminally truncated 14-3-3 gamma

14-3-3 protein gamma
MWexperimental 51 kDa
MWexpected 54 kDa
VPorod 76 nm3
log I(s) 5.97×10-2 5.97×10-3 5.97×10-4 5.97×10-5
14-3-3 protein gamma small angle scattering data  s, nm-1
ln I(s)
14-3-3 protein gamma Guinier plot ln 5.97×10-2 Rg: 2.8 nm 0 (2.8 nm)-2 s2
(sRg)2I(s)/I(0)
14-3-3 protein gamma Kratky plot 1.104 0 √3 sRg
p(r)
14-3-3 protein gamma pair distance distribution function Rg: 2.8 nm 0 Dmax: 8.4 nm

Data validation

Fits and models

log I(s)
 s, nm-1
14-3-3 protein gamma PDB (PROTEIN DATA BANK) model
log I(s)
 s, nm-1
14-3-3 protein gamma DAMMIN model
Synchrotron SAXS data from solutions of human phosphorylated CaMKK1 bound to 14-3-3 gamma in 50 mM Tris-HCl, 150 mM NaCl, 1 mM TCEP, 3% (w/v) glycerol, pH 7.5 were collected on the EMBL P12 beam line at PETRA III (DESY; Hamburg, Germany) using a Pilatus 2M detector at a sample-detector distance of 3 m and at a wavelength of λ = 0.123987 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 48.00 μl sample at 6 mg/ml was injected at a 0.30 ml/min flow rate onto a GE Superdex 200 Increase 5/150 column at 20°C. 1320 successive 0.495 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.

14-3-3 protein gamma (14-3-3gamma)
Mol. type   Protein
Organism   Homo sapiens
Olig. state   Dimer
Mon. MW   27.0 kDa
 
UniProt   P61981 (1-234)
Sequence   FASTA
 
PDB ID   2B05