Structural and functional studies of the Leishmania braziliensis mitochondrial Hsp70: Similarities and dissimilarities to human orthologues.

Dores-Silva PR, Nishimura LS, Kiraly VT, Borges JC, Arch Biochem Biophys 613:43-52 (2017) Europe PMC

SASDBY6 – Leishmania braziliensis Mitochondrial heat shock protein 70 (LbmtHSP70)

Mitochondrial heat shock protein 70
MWI(0) 76 kDa
MWexpected 71 kDa
VPorod 118 nm3
log I(s) 2.52×10-2 2.52×10-3 2.52×10-4 2.52×10-5
Mitochondrial heat shock protein 70 small angle scattering data  s, nm-1
ln I(s)
Mitochondrial heat shock protein 70 Guinier plot ln 2.53×10-2 Rg: 3.6 nm 0 (3.6 nm)-2 s2
(sRg)2I(s)/I(0)
Mitochondrial heat shock protein 70 Kratky plot 1.104 0 √3 sRg
p(r)
Mitochondrial heat shock protein 70 pair distance distribution function Rg: 3.8 nm 0 Dmax: 14 nm

Data validation

Fits and models

log I(s)
 s, nm-1
Mitochondrial heat shock protein 70 DAMMIN model
Synchrotron SAXS data from solutions of Leishmania braziliensis mitochondrial heat shock protein 70 (LbmtHSP70) in 25 mM Tris-HCl, 50 mM NaCL, 5 mM KCl, 5 mM sodium phosphate, 2 mM β-mercaptoethanol, pH 7.5, were collected on the SAXS1 Beamline at the Brazilian Synchrotron Light Laboratory (Campinas, Brazil) using a 20Hz Pilatus 300K detector at a sample-detector distance of 1 m and at a wavelength of λ = 0.1488 nm (I(s) vs s, where s = 4π sin θ/λ and 2θ is the scattering angle). Scattering data from solute concentration of 0.5 mg/ml was measured at 25°C. Five successive 60 second data frames were collected. The data were normalized to the intensity of the transmitted beam and radially averaged; the radially-averaged scattering of the solvent-blank was subtracted.

Mitochondrial heat shock protein 70 (LbmtHsp70)
Mol. type   Protein
Organism   Leishmania braziliensis
Olig. state   Monomer
Mon. MW   70.9 kDa
Sequence   FASTA