Low resolution structural studies indicate that the activator of Hsp90 ATPase 1 (Aha1) of Leishmania braziliensis has an elongated shape which allows its interaction with both N- and M-domains of Hsp90.

Seraphim TV, Alves MM, Silva IM, Gomes FE, Silva KP, Murta SM, Barbosa LR, Borges JC, PLoS One 8(6):e66822 (2013) Europe PMC

SASDBR4 – Leishmania braziliensis Activator of Hsp90 ATPase-1 (LbAha1)

Activator of Hsp90 ATPase-1
MWexperimental 47 kDa
MWexpected 38 kDa
log I(s) 3.00×10-2 3.00×10-3 3.00×10-4 3.00×10-5
Activator of Hsp90 ATPase-1 small angle scattering data  s, nm-1
ln I(s)
Activator of Hsp90 ATPase-1 Guinier plot ln 3×10-2 Rg: 3.6 nm 0 (3.6 nm)-2 s2
(sRg)2I(s)/I(0)
Activator of Hsp90 ATPase-1 Kratky plot 1.104 0 √3 sRg
p(r)
Activator of Hsp90 ATPase-1 pair distance distribution function Rg: 3.9 nm 0 Dmax: 14.5 nm

Data validation

Fits and models

log I(s)
 s, nm-1
Leishmania braziliensis Activator of Hsp90 ATPase-1 (LbAha1) Rg histogram Rg, nm
Activator of Hsp90 ATPase-1 EOM/RANCH model
log I(s)
 s, nm-1
Activator of Hsp90 ATPase-1 DAMMIN model
Synchrotron SAXS data from solutions of Leishmania braziliensis Activator of Hsp90 ATPase-1 in 50 mM sodium phosphate, 50 mM NaCl, 2 mM EDTA, 1 mM β-mercaptoethanol, pH 7, were collected on the SAXS2 Beamline camera on the storage ring Brazilian Synchrotron Light Laboratory (Campinas, Brazil) using a MAR Image Plate detector (I(s) vs s; s = 4π sin θ/λ, where 2θ is the scattering angle and λ=0.1488 nm). Different solute concentrations in the range 1.10-3.20 mg/ml were measured. Three successive 300 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 and the different curves were scaled for protein concentration. The low angle data collected were merged with the highest concentration high angle data to yield the final composite scattering curve. The Ensemble Optimization Method (EOM) model displayed in this entry is a structural representative from a final refined pool of flexible structures. Additional EOM results, including the Rg and Dmax distributions from two EOM modelling runs, are included in the full entry zip archive.

Ab initio model of Leishmania braziliensis Activator of Hsp90 ATPase-1 (LbAha1) and Ensemble Optimization Method analysis on LbAha1 conformational dynamics. Results showed that LbAha1 is remarkably flexible.

Activator of Hsp90 ATPase-1 (LbAha1)
Mol. type   Protein
Organism   Leishmania braziliensis
Olig. state   Monomer
Mon. MW   38.3 kDa
Sequence   FASTA