Allosteric regulation of deubiquitylase activity through ubiquitination.

Faggiano S, Menon RP, Kelly GP, Todi SV, Scaglione KM, Konarev PV, Svergun DI, Paulson HL, Pastore A, Front Mol Biosci 2:2 (2015) Europe PMC

SASDLP5 – Complex of the josephin domain of ataxin-3 with ubiquitin

Josephin domain of ataxin-3
Polyubiquitin-B
MWexperimental 30 kDa
MWexpected 29 kDa
VPorod 45 nm3
log I(s) 3.60×103 3.60×102 3.60×101 3.60×100
Josephin domain of ataxin-3 Polyubiquitin-B small angle scattering data  s, nm-1
ln I(s)
Josephin domain of ataxin-3 Polyubiquitin-B Guinier plot ln 3.60×103 Rg: 2.1 nm 0 (2.1 nm)-2 s2
(sRg)2I(s)/I(0)
Josephin domain of ataxin-3 Polyubiquitin-B Kratky plot 1.104 0 √3 sRg
p(r)
Josephin domain of ataxin-3 Polyubiquitin-B pair distance distribution function Rg: 2.1 nm 0 Dmax: 6.5 nm

Data validation

Fits and models

log I(s)
 s, nm-1
Josephin domain of ataxin-3 Polyubiquitin-B DAMMIF model
log I(s)
 s, nm-1
Josephin domain of ataxin-3 Polyubiquitin-B SASREF model
Synchrotron SAXS data from solutions of the complex formed between the josephin domain of ataxin-3 with ubiquitin in 20 mM Na-phosphate buffer, 2 mM DTT, pH 6.5 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 3.1 m and at a wavelength of λ = 0.125 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). One solute concentration of 5.97 mg/ml was measured. 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.

Cell temperature = UNKNOWN. Storage temperature = UNKNOWN

Josephin domain of ataxin-3 (josephin domain)
Mol. type   Protein
Organism   Homo sapiens
Olig. state   Monomer
Mon. MW   20.9 kDa
Sequence   FASTA
 
Polyubiquitin-B (Ubiquitin)
Mol. type   Protein
Organism   Homo sapiens
Olig. state   Monomer
Mon. MW   8.6 kDa
 
UniProt   P0CG47 (1-76)
Sequence   FASTA