N-terminal phosphorylation regulates the activity of glycogen synthase kinase 3 from Plasmodium falciparum.

Pazicky S, Alder A, Mertens H, Svergun D, Gilberger T, Löw C, Biochem J 479(3):337-356 (2022) Europe PMC

SASDL87 – Plasmodium falciparum Glycogen Synthase Kinase 3 - Ion Exchange Chromatography Fraction 4

Glycogen synthase kinase 3
MWexperimental 49 kDa
MWexpected 52 kDa
VPorod 101 nm3
log I(s) 2.08×10-2 2.08×10-3 2.08×10-4 2.08×10-5
Glycogen synthase kinase 3 small angle scattering data  s, nm-1
ln I(s)
Glycogen synthase kinase 3 Guinier plot ln 2.09×10-2 Rg: 3.2 nm 0 (3.2 nm)-2 s2
(sRg)2I(s)/I(0)
Glycogen synthase kinase 3 Kratky plot 1.104 0 √3 sRg
p(r)
Glycogen synthase kinase 3 pair distance distribution function Rg: 3.3 nm 0 Dmax: 11.6 nm

Data validation

Fits and models

log I(s)
 s, nm-1
Glycogen synthase kinase 3 CORAL model
Synchrotron SAXS data from solutions of P. falciparum glycogen synthase kinase 3 in 20 mM Tris pH 8.0, 100 mM NaCl, 0.5 mM TCEP were collected on the EMBL P12 beam line at PETRA III (DESY, Hamburg, Germany) using a Pilatus 6M detector at a sample-detector distance of 3 m and at a wavelength of λ = 0.124 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 30.00 μl sample at 10 mg/ml was injected at a 0.40 ml/min flow rate onto a GE Superdex 200 Increase 5/150 column at 20°C. 23 successive 0.995 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.

Glycogen synthase kinase 3 (PfGSK3)
Mol. type   Protein
Organism   Plasmodium falciparum (isolate 3D7)
Olig. state   Monomer
Mon. MW   52.0 kDa
 
UniProt   O77344 (1-440)
Sequence   FASTA