Identification of two p23 co-chaperone isoforms in Leishmania braziliensis exhibiting similar structures and Hsp90 interaction properties despite divergent stabilities.

Batista FA, Almeida GS, Seraphim TV, Silva KP, Murta SM, Barbosa LR, Borges JC, FEBS J 282(2):388-406 (2015) Europe PMC

SASDC85 – Leishmania braziliensis p23B

Leishmania braziliensis p23 isoform B
MWexperimental 26 kDa
MWexpected 23 kDa
log I(s) 2.00×10-2 2.00×10-3 2.00×10-4 2.00×10-5
Leishmania braziliensis p23 isoform B small angle scattering data  s, nm-1
ln I(s)
Leishmania braziliensis p23 isoform B Guinier plot ln 2.01×10-2 Rg: 3.0 nm 0 (3.0 nm)-2 s2
(sRg)2I(s)/I(0)
Leishmania braziliensis p23 isoform B Kratky plot 1.104 0 √3 sRg
p(r)
Leishmania braziliensis p23 isoform B pair distance distribution function Rg: 3.2 nm 0 Dmax: 13 nm

Data validation

Fits and models

log I(s)
 s, nm-1
Leishmania braziliensis p23 isoform B DAMFILT model
SAXS experiments were performed at the SAXS2 beam line in the Laboratório Nacional de Luz Síncrotron (LNLS, Campinas-SP, 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 MAR-CCD detector. Measurements were performed with a monochromatic X-ray beam and a sample-to-detector distance of ~1000 mm, corresponding to a scattering vector range of 0.015 < q < 0.35 Å−1. Scattering patterns were recorded at different sample concentrations (approximately 1.0, 2.0 and 4.0 mg/mL) and several frames in order to check for protein aggregation and X-ray damage. No evidence of aggregation or inter-particle interference were observed. The model depicts the averaged spatial representation of the protein (DAMFILT occupancy and volume-corrected bead model).

Number of frames = UNKNOWN

Leishmania braziliensis p23 isoform B (Lbp23B)
Mol. type   Protein
Organism   Leishmania braziliensis
Olig. state   Monomer
Mon. MW   23.0 kDa
 
UniProt   A4HAD9
Sequence   FASTA