Atomic structure of the Leishmania spp. Hsp100 N‐domain

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. Whethe...

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Bibliographic Details
Published in:Proteins, structure, function, and bioinformatics structure, function, and bioinformatics, 2022-06, Vol.90 (6), p.1242-1246
Main Authors: Mercado, Jonathan M., Lee, Sukyeong, Chang, Changsoo, Sung, Nuri, Soong, Lynn, Catic, Andre, Tsai, Francis T. F.
Format: Article
Language:English
Subjects:
Amino acids
Atomic structure
Binding Sites
Crystal structure
Disaggregation
Domains
Heat-Shock Proteins - chemistry
Hsp100
Humans
Immune system
Leishmania
Leishmania - metabolism
Leishmaniasis
Malaria
molecular chaperone
Molecular Chaperones - chemistry
Peptides - chemistry
Polypeptides
Protein transport
protein unfoldase
Proteins
Substrates
Therapeutic targets
Tropical diseases
Vector-borne diseases
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Summary: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.
ISSN:0887-3585
1097-0134
DOI:10.1002/prot.26310