Atomic structure of the Leishmania spp. Hsp100 N-domain
We report 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 angstrom 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.
- Research Organization:
- Argonne National Laboratory (ANL), Argonne, IL (United States)
- Sponsoring Organization:
- USDOE Office of Science (SC), Basic Energy Sciences (BES); Welch Foundation; National Institutes of Health (NIH); Cancer Prevention and Research Institute of Texas; Gulf Coast Consortia on the Houston Area Molecular Biophysics Program
- Grant/Contract Number:
- AC02-06CH11357
- OSTI ID:
- 1870154
- Journal Information:
- Proteins, Journal Name: Proteins Journal Issue: 6 Vol. 90; ISSN 0887-3585
- Publisher:
- WileyCopyright Statement
- Country of Publication:
- United States
- Language:
- English
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