Atomic structure of the Leishmania spp. Hsp100 N-domain.
Hsp100
Leishmania
molecular chaperone
protein unfoldase
Journal
Proteins
ISSN: 1097-0134
Titre abrégé: Proteins
Pays: United States
ID NLM: 8700181
Informations de publication
Date de publication:
06 2022
06 2022
Historique:
revised:
14
01
2022
received:
29
11
2021
accepted:
01
02
2022
pubmed:
6
2
2022
medline:
21
4
2022
entrez:
5
2
2022
Statut:
ppublish
Résumé
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.
Identifiants
pubmed: 35122310
doi: 10.1002/prot.26310
pmc: PMC9018533
mid: NIHMS1777116
doi:
Substances chimiques
Heat-Shock Proteins
0
Molecular Chaperones
0
Peptides
0
Types de publication
Journal Article
Research Support, U.S. Gov't, Non-P.H.S.
Research Support, N.I.H., Extramural
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
1242-1246Subventions
Organisme : NIGMS NIH HHS
ID : T32 GM008280
Pays : United States
Organisme : NIGMS NIH HHS
ID : R01 GM104980
Pays : United States
Organisme : NIDDK NIH HHS
ID : R01 DK115454
Pays : United States
Organisme : NIAID NIH HHS
ID : R01 AI130126
Pays : United States
Organisme : NIH HHS
ID : S10 OD030246
Pays : United States
Organisme : NIGMS NIH HHS
ID : R01 GM142143
Pays : United States
Informations de copyright
© 2022 Wiley Periodicals LLC.
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