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Structural characterization of protozoa Hsp100 by single-particle cryo-transmission electron microscopy (Cryo-TEM).


EMSL Project ID
51612

Abstract

Chaperones, such as Hsp100, can help maintain cellular homeostasis and adaptation playing an important role for different organisms. The Hsp100 has a disaggregase action, acting with other proteins of the chaperone system to extract polypeptides from protein aggregates, allowing their unfolding and subsequent refolding, avoiding their toxic effect on the cell. Moreover, Hsp100 appears to be essential for human pathogens microorganisms like Leishmania sp. and Plasmodium sp. Recently reports suggested that Hsp100 is hexameric and present a conformation change in complex with nucleotides. Here, we plan to obtain the atomic resolution of the essential Leishmania braziliensis Hsp100 apo and in complex with adenosine nucleotides. These results will increase the current understanding on chaperones in this microorganism and its role during cell-invasion.

Project Details

Start Date
2020-10-19
End Date
2021-03-17
Status
Closed

Team

Principal Investigator

Julio Borges
Institution
Sao Carlos Institute of Chemistry, University of Sao Paulo

Team Members

Sean Mulligan
Institution
Oregon Health & Science University

Vitor Hugo Balasco Serrão
Institution
University of California, Santa Cruz

Jessica Fernandes Scortecci
Institution
The University of British Columbia

Irina El Khoury
Institution
Environmental Molecular Sciences Laboratory