Structural and functional studies of the Leishmania braziliensis SGT co-chaperone indicate that it shares structural features with HIP and can interact with both Hsp90 and Hsp70 with similar affinities.

Coto ALS, Seraphim TV, Batista FAH, Dores-Silva PR, Barranco ABF, Teixeira FR, Gava LM, Borges JC, Int J Biol Macromol 118(Pt A):693-706 (2018) PubMed

SASDC75 – Leishmania braziliensis SGT co-chaperone

SGT protein
MWI(0) 102 kDa
MWexpected 92 kDa
log I(s) 6.59×10-2 6.59×10-3 6.59×10-4 6.59×10-5
SGT protein small angle scattering data  s, nm-1
ln I(s)
SGT protein Guinier plot ln 6.59×10-2 Rg: 4.5 nm 0 (4.5 nm)-2 s2
SGT protein Kratky plot 1.104 0 3 sRg
SGT protein pair distance distribution function Rg: 4.7 nm 0 Dmax: 17 nm

Experimental data validation

Fits and models

log I(s)
 s, nm-1
SGT protein DAMFILT model
SAXS experiments were performed at the D02A-SAXS2 beamline at the Brazilian Synchrotron Light Laboratory (LNLS, Campinas, São Paulo, Brazil). The X-ray scattering data (I(s) vs s, where s = 4πsinθ/λ and 2θ is the scattering angle; λ = 0.1488 nm) were acquired using a two-dimensional position-sensitive MAR-CCD detector. Measurements were performed using a monochromatic X-ray beam and a sample-to-detector distance of ~1,000 mm, corresponding to the scattering vector range of 0.015 < q < 0.35 Å-1. LbSGT samples were prepared at 1.5 mg/mL, 3.0 mg/mL, 4.5 mg/mL and 6.0 mg/mL. Successive frames (20, 60 and 300 sec) were collected to inspect for X-ray damage. Aggregation or inter-particle interference were not observed. The model depicts the averaged spatial representation of the protein (DAMFILT occupancy and volume-corrected bead model).

SGT protein (LbSGT)
Mol. type   Protein
Organism   Leishmania braziliensis
Olig. state   Dimer
Mon. MW   45.9 kDa
UniProt   A4HIK6
Sequence   FASTA