Intramolecular Interactions between Folded and Disordered Regions Shape Ubiquilin Structure and Function

Niblo J, Acharya N, Watkins M, Castañeda C Sukenik S, Advanced Science (2026) DOI

SASDZB9 – Full-length yeast shuttle protein Dsk2 with single point mutation (I45A)

Ubiquitin domain-containing protein DSK2 I45A
MWexperimental 38 kDa
MWexpected 39 kDa
log I(s) 1.62×10-2 1.62×10-3 1.62×10-4 1.62×10-5
Ubiquitin domain-containing protein DSK2 I45A small angle scattering data  s, nm-1
ln I(s)
Ubiquitin domain-containing protein DSK2 I45A Guinier plot ln 1.62×10-2 Rg: 3.9 nm 0 (3.9 nm)-2 s2
(sRg)2I(s)/I(0)
Ubiquitin domain-containing protein DSK2 I45A Kratky plot 1.104 0 √3 sRg

Data validation

There are no models related to this curve.

Synchrotron SAXS data from solutions of Full-length yeast shuttle protein Dsk2 with single point mutation (I45A) in 20 mM sodium phosphate, 0.5 mM EDTA, 0.02% NaN3, pH 6.8 were collected on the BioCAT 18ID beam line at the Advanced Photon Source (APS), Argonne National Laboratory storage ring (Lemont, IL, USA) using a Pilatus3 X 1M detector at a sample-detector distance of 3.7 m and at a wavelength of λ = 1.03325 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 200.00 μl sample at 6.1 mg/ml was injected at a 0.60 ml/min flow rate onto a GE Superdex 200 Increase 10/300 column at 23.9°C. 2470 successive 0.500 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.

Ubiquitin domain-containing protein DSK2 I45A (DSK2 I45A)
Mol. type   Protein
Organism   Saccharomyces cerevisiae
Olig. state   Monomer
Mon. MW   39.3 kDa
 
UniProt   P48510
Sequence   FASTA