Low sequence identity but high structural and functional conservation: The case of Hsp70/Hsp90 organizing protein (Hop/Sti1) of Leishmania braziliensis.

Batista FAH, Seraphim TV, Santos CA, Gonzaga MR, Barbosa LRS, Ramos CHI, Borges JC, Arch Biochem Biophys 600:12-22 (2016) Europe PMC

SASDB54 – Leishmania braziliensis stress-induced protein sti1 (LbHop), full length construct

Stress-induced protein sti1
MWexperimental 63 kDa
MWexpected 62 kDa
VPorod 94 nm3
log I(s) 6.30×10-2 6.30×10-3 6.30×10-4 6.30×10-5
Stress-induced protein sti1 small angle scattering data  s, nm-1
ln I(s)
Stress-induced protein sti1 Guinier plot ln 6.30×10-2 Rg: 4.5 nm 0 (4.5 nm)-2 s2
(sRg)2I(s)/I(0)
Stress-induced protein sti1 Kratky plot 1.104 0 √3 sRg
p(r)
Stress-induced protein sti1 pair distance distribution function Rg: 4.7 nm 0 Dmax: 18 nm

Data validation

Fits and models

log I(s)
 s, nm-1
Stress-induced protein sti1 DAMFILT model
X-ray synchrotron radiation scattering data from solutions of stress-induced protein sti1 (Hop/Sti1) in 25 mM Tris 100 mM NaCl, 1 mM EDTA, 1 mM β-mercaptoethanol were collected on the SAXS1 and SAXS2 beam lines at the Brazilian Synchrotron Light Laboratory (Campinas, Brazil) using a MAR Image Plate and Pilatus 300k detectors (s = 4π sin θ/λ, where 2θ is the scattering angle). Different solute concentrations in the range 0.80-1.80 mg/ml were measured. The data were normalized to the intensity of the transmitted beam and radially averaged; the scattering of the solvent-blank was subtracted and the different curves were scaled for protein concentration. The low angle data collected were merged to yield the final composite scattering curve.

Wavelength = UNKNOWN. Cell temperature = UNKNOWN. Storage temperature = UNKNOWN. Sample detector distance = UNKNOWN. X-ray Exposure time = UNKNOWN. Number of frames = UNKNOWN

Stress-induced protein sti1 (Hop/Sti1)
Mol. type   Protein
Organism   Leishmania braziliensis
Olig. state   Monomer
Mon. MW   62.5 kDa
 
UniProt   A4H5F0 (1-547)
Sequence   FASTA