Structural-functional diversity of malaria parasite's PfHSP70-1 and PfHSP40 chaperone pair gives an edge over human orthologs in chaperone-assisted protein folding.

Anas M, Shukla A, Tripathi A, Kumari V, Prakash C, Nag P, Kumar LS, Sharma SK, Ramachandran R, Kumar N
Biochem J 477(18):3625-3643 (2020 Sep 30)
PMID: 32893851
doi: 10.1042/BCJ20200434 		Submitted to SASBDB: 2020 Feb 7
Published in SASBDB:

SASDHU5 – Heat shock protein 70 (PfHSP70-1)

Heat shock protein 70Peptide experimental SAS data
DAMFILT model
Sample: Heat shock protein 70 monomer, 74 kDa Plasmodium falciparum protein
Peptide monomer, 1 kDa synthetic construct protein
Buffer: 50mM Tris, 5mM MgCl2, 500mM KCl, 5mM Bme, 5% glycerol, pH: 8
Experiment: SAXS data collected at Anton Paar SAXSpace, CSIR-Central Drug Research Institute on 2019 Oct 24
RgGuinier 5.3 nm
Dmax 16.6 nm
VolumePorod 450 nm3

SASDHR5 – Heat shock protein 40, subfamily A (PfHSP40)

HSP40, subfamily A experimental SAS data
DAMMIF model
Sample: HSP40, subfamily A dimer, 97 kDa Plasmodium falciparum protein
Buffer: 50 mM Tris, 5 mM MgCl2, 300 mM KCl, 1 mM β-mercaptoethanol, 5% glycerol, pH: 8
Experiment: SAXS data collected at Anton Paar SAXSpace, CSIR-Central Drug Research Institute on 2019 Oct 24
RgGuinier 4.3 nm
Dmax 15.0 nm
VolumePorod 339 nm3