Interactions of ataxin-3 with its molecular partners in the protein machinery that sorts protein aggregates to the aggresome.

Bonanomi M, Mazzucchelli S, D'Urzo A, Nardini M, Konarev PV, Invernizzi G, Svergun DI, Vanoni M, Regonesi ME, Tortora P, Int J Biochem Cell Biol 51:58-64 (2014) Europe PMC

SASDLK5 – Aggregation state of ataxin-3-tubulin complex

Ataxin-3
Tubulin alpha-1A chain
MWI(0) 490 kDa
MWexpected 91 kDa
VPorod 900 nm3
log I(s) 3.15×102 3.15×101 3.15×100 3.15×10-1
Ataxin-3 Tubulin alpha-1A chain small angle scattering data  s, nm-1
ln I(s)
Ataxin-3 Tubulin alpha-1A chain Guinier plot ln 3.16×102 Rg: 8.4 nm 0 (8.4 nm)-2 s2
(sRg)2I(s)/I(0)
Ataxin-3 Tubulin alpha-1A chain Kratky plot 1.104 0 √3 sRg
p(r)
Ataxin-3 Tubulin alpha-1A chain pair distance distribution function Rg: 8.4 nm 0 Dmax: 30 nm

Data validation

Fits and models

log I(s)
 s, nm-1
Ataxin-3 Tubulin alpha-1A chain DAMMIN model
Synchrotron SAXS data from solutions of an ataxin-3-tubulin assembly in phosphate buffered saline (PBS), pH 7.4 were collected on the EMBL X33 beam line at DORIS III (DESY, Hamburg, Germany) using a Pilatus 1M-W detector at a sample-detector distance of 2.7 m and at a wavelength of λ = 0.154 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). One solute concentration of 11.25 mg/ml was measured at 10°C. Four successive 30 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.

Tags: X33
Ataxin-3 (ATQ24)
Mol. type   Protein
Organism   Homo sapiens
Olig. state   Monomer
Mon. MW   41.3 kDa
 
UniProt   P54252 (1-361)
Sequence   FASTA
 
Tubulin alpha-1A chain (Tubulin)
Mol. type   Protein
Organism   Homo sapiens
Olig. state   Monomer
Mon. MW   50.1 kDa
 
UniProt   Q71U36 (1-451)
Sequence   FASTA