Breakthrough Shines Light on Protein Chaperones
February 5, 2019Feature Story
A team of researchers have obtained the highest-resolution structure of the fungal protein Hsp104, which could be used to hinder the formation of certain degenerative diseases. Using the Advanced Photon Source at Argonne National Laboratory, the researchers combined X-ray crystallography and cryo-electron microscopy (cryo-EM) to also verify that these protein-formed hexamers, once believed flat, have a helical structure. Known as a chaperone, the hexameric AAA+ protein Hsp104 helps in the natural folding processes of proteins for proper cell function and may be able to repair misfolded or aggregated proteins that can lead to protein-caused abnormalities.
Michalska, K., et al. 2019. “Structure of Calcarisporiella thermophila Hsp104 Disaggregase that Antagonizes Diverse Proteotoxic Misfolding Events,” Structure 27(3), 449–63. [DOI:10.1016/j.str.2018.11.001]