Language
English
Publication Date
6-1-2022
Journal
Proteins
DOI
10.1002/prot.26310
PMID
35122310
PMCID
PMC9018533
PubMedCentral® Posted Date
12-1-2022
PubMedCentral® Full Text Version
Author MSS
Abstract
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
Binding Sites, Heat-Shock Proteins, Humans, Peptides, Leishmania, Molecular chaperone, Protein unfoldase, Hsp100
Published Open-Access
yes
Recommended Citation
Mercado, Jonathan M; Lee, Sukyeong; Chang, Changsoo; et al., "Atomic Structure of the Leishmania spp Hsp100 N-domain" (2022). Faculty and Staff Publications. 115.
https://digitalcommons.library.tmc.edu/baylor_docs/115