6ZHI

Structure of the Plasmodium falciparum Hsp70-x substrate binding domain in complex with hydrophobic peptide

Summary for 6ZHI

• Entry DOI: 10.2210/pdb6zhi/pdb
• Descriptor: Heat shock protein 70, ASN-ARG-LEU-LEU-LEU-THR-GLY (2 entities in total)
• Functional Keywords: malaria, erythrocyte remodelling, pfhsp70-x, complex, chaperone
• Biological source: Plasmodium falciparum (isolate 3D7); More
• Total number of polymer chains: 8
• Total formula weight: 106491.63

Authors

Schmidt, J.,Vakonakis, I. (deposition date: 2020-06-23, release date: 2020-09-09, Last modification date: 2024-09-25)

Primary citation

Schmidt, J.,Vakonakis, I.
Structure of the substrate-binding domain of Plasmodium falciparum heat-shock protein 70-x.
Acta Crystallogr.,Sect.F, 76:495-500, 2020

PubMed Abstract: The malaria parasite Plasmodium falciparum extensively modifies erythrocytes that it invades by exporting a large complement of proteins to the host cell. Among these exported components is a single heat-shock 70 kDa class protein, PfHsp70-x, that supports the virulence and growth rate of the parasite during febrile episodes. The ATP-binding domain of PfHsp70-x has previously been resolved and showed the presence of potentially druggable epitopes that differ from those on human Hsp70 chaperones. Here, the crystallographic structure of the substrate-binding domain (SBD) of PfHsp70-x is presented in complex with a hydrophobic peptide. The PfHsp70-x SBD is shown to be highly similar to the counterpart from a human erythrocytic Hsp70 chaperone. The binding of substrate at the interface between β-sandwich and α-helical subdomains of this chaperone segment is also conserved between the malaria parasite and humans. It is hypothesized that the parasite may partly exploit human chaperones for intra-erythrocytic trafficking and maintenance of its exported proteome.

PubMed: 33006578
DOI: 10.1107/S2053230X2001208X

Experimental method

X-RAY DIFFRACTION (3.25 Å)