Atomic structure of the Leishmania spp. Hsp100 N-domain

Jonathan M. Mercado, Sukyeong Lee, Changsoo Chang, Nuri Sung, Lynn Soong, Andre Catic, Francis T.F. Tsai

Research output: Contribution to journalArticlepeer-review


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.

Original languageEnglish (US)
Pages (from-to)1242-1246
Number of pages5
JournalProteins: Structure, Function and Bioinformatics
Issue number6
StatePublished - Jun 2022
Externally publishedYes


  • Hsp100
  • Leishmania
  • molecular chaperone
  • protein unfoldase

ASJC Scopus subject areas

  • Structural Biology
  • Biochemistry
  • Molecular Biology


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