Atomic structure of the Leishmania spp. Hsp100 N-domain

Proteins. 2022 Jun;90(6):1242-1246. doi: 10.1002/prot.26310. Epub 2022 Feb 18.


Hsp100 is an ATP-dependent unfoldase that promotes protein disaggregation or facilitates the unfolding of aggregation-prone polypeptides marked for degradation. Recently, new Hsp100 functions are emerging. In Plasmodium, an Hsp100 drives malaria protein export, presenting a novel drug target. Whether Hsp100 has a similar function in other protists is unknown. We present the 1.06 Å resolution crystal structure of the Hsp100 N-domain from Leishmania spp., the causative agent of leishmaniasis in humans. Our structure reveals a network of methionines and aromatic amino acids that define the putative substrate-binding site and likely evolved to protect Hsp100 from oxidative damage in host immune cells.

Keywords: Hsp100; Leishmania; molecular chaperone; protein unfoldase.

Publication types

  • Research Support, U.S. Gov't, Non-P.H.S.
  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Binding Sites
  • Heat-Shock Proteins* / chemistry
  • Humans
  • Leishmania* / metabolism
  • Molecular Chaperones / chemistry
  • Peptides / chemistry


  • Heat-Shock Proteins
  • Molecular Chaperones
  • Peptides