Environmental Molecular Sciences Laboratory

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

Monday, October 19, 2020
Principal Investigator: 
Julio Borges
Lead Institution: 
Sao Carlos Institute of Chemistry, University of Sao Paulo
Project ID: 

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.