Senescence-associated ubiquitin ligase 1 (SAUL1)

Haifa El Kilani, Al Kikhney.

SASDEU3 – GST-SAUL1

Senescence-associated E3 ubiquitin ligase 1
Glutathione S-transferase
MWexperimental 486 kDa
MWexpected 461 kDa
VPorod 778 nm3
log I(s) 1.73×103 1.73×102 1.73×101 1.73×100
Senescence-associated E3 ubiquitin ligase 1 Glutathione S-transferase small angle scattering data  s, nm-1
ln I(s)
Senescence-associated E3 ubiquitin ligase 1 Glutathione S-transferase Guinier plot ln 1.73×103 Rg: 7.6 nm 0 (7.6 nm)-2 s2
(sRg)2I(s)/I(0)
Senescence-associated E3 ubiquitin ligase 1 Glutathione S-transferase Kratky plot 1.104 0 √3 sRg
p(r)
Senescence-associated E3 ubiquitin ligase 1 Glutathione S-transferase pair distance distribution function Rg: 7.8 nm 0 Dmax: 28 nm

Data validation

Fits and models

log I(s)
 s, nm-1
Senescence-associated E3 ubiquitin ligase 1 Glutathione S-transferase CORAL model
log I(s)
 s, nm-1
Senescence-associated E3 ubiquitin ligase 1 Glutathione S-transferase DAMMIF model
Synchrotron SAXS data from solutions of GST-SAUL1 in 50 mM Tris, 250 mM NaCl, pH 9 were collected on the EMBL P12 beam line at the PETRA III storage ring (DESY; Hamburg, Germany) using a Pilatus 2M detector at a sample-detector distance of 3 m and at a wavelength of λ = 0.123956 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). One solute concentration of 1.00 mg/ml was measured at 23°C. 20 successive 0.050 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.

The rigid bodies used for the SAUL1 tetramer model were predicted by I-TASSER.

Senescence-associated E3 ubiquitin ligase 1 (SAUL1)
Mol. type   Protein
Organism   Arabidopsis thaliana
Olig. state   Tetramer
Mon. MW   88.8 kDa
 
UniProt   Q9LM76
Sequence   FASTA
 
Glutathione S-transferase (GST)
Mol. type   Protein
Organism   Schistosoma japonicum
Olig. state   Tetramer
Mon. MW   26.4 kDa
 
UniProt   P08515
Sequence   FASTA
 
PDB ID   3BBY