Human stress-inducible Hsp70 has a high propensity to form ATP-dependent antiparallel dimers that are differentially regulated by co-chaperone binding.

Trcka F, Durech M, Vankova P, Chmelik J, Martinkova V, Hausner J, Kadek A, Marcoux J, Klumpler T, Vojtesek B, Muller P, Man P, Mol Cell Proteomics (2018) Europe PMC

SASDDN6 – Human stress-inducible heat shock 70 kDa protein 1, Hsp70 (Hspa1a) T204A mutant dimer, in the presence of ATP

Heat shock 70 kDa protein 1
MWexperimental 148 kDa
MWexpected 147 kDa
VPorod 248 nm3
log I(s) 7.60×10-1 7.60×10-2 7.60×10-3 7.60×10-4
Heat shock 70 kDa protein 1 small angle scattering data  s, nm-1
ln I(s)
Heat shock 70 kDa protein 1 Guinier plot ln 7.60×10-1 Rg: 4.0 nm 0 (4.0 nm)-2 s2
Heat shock 70 kDa protein 1 Kratky plot 1.104 0 3 sRg
Heat shock 70 kDa protein 1 pair distance distribution function Rg: 4.0 nm 0 Dmax: 11.6 nm

Data validation

Fits and models

log I(s)
 s, nm-1
Heat shock 70 kDa protein 1 MODELLER model

SAXS data from solutions of human stress-induced heat shock 70 kDa protein 1 ,Hsp70, (Hspa1a T204A mutant), with ATP in 50mM HEPES; 150mM KCH3COO; 2mM MgCl2, pH 7.5, were collected on a Rigaku BioSAXS-1000 instrument at CEITEC (Brno, Czech Republic) using a Pilatus 100K detector at a sample-detector distance of 0.5 m and at a wavelength of λ = 0.154 nm (l(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). One solute concentration of 2.50 mg/ml was measured at 4°C. The data were normalized to the intensity of the transmitted beam and radially averaged; the scattering of the solvent-blank was subtracted.

Heat shock 70 kDa protein 1 (HSPA1A_T204A)
Mol. type   Protein
Organism   Homo sapiens
Olig. state   Dimer
Mon. MW   73.7 kDa
UniProt   P0DMV8
Sequence   FASTA