Structural basis for aggregate dissolution and refolding by the Mycobacterium tuberculosis ClpB-DnaK bi-chaperone system.
ClpB disaggregase
DnaK chaperone
Mycobacterium tuberculosis
cryo-EM
structural biology
Journal
Cell reports
ISSN: 2211-1247
Titre abrégé: Cell Rep
Pays: United States
ID NLM: 101573691
Informations de publication
Date de publication:
25 05 2021
25 05 2021
Historique:
received:
11
05
2020
revised:
30
12
2020
accepted:
03
05
2021
entrez:
26
5
2021
pubmed:
27
5
2021
medline:
11
2
2022
Statut:
ppublish
Résumé
The M. tuberculosis (Mtb) ClpB is a protein disaggregase that helps to rejuvenate the bacterial cell. DnaK is a protein foldase that can function alone, but it can also bind to the ClpB hexamer to physically couple protein disaggregation with protein refolding, although the molecular mechanism is not well understood. Here, we report the cryo-EM analysis of the Mtb ClpB-DnaK bi-chaperone in the presence of ATPγS and a protein substrate. We observe three ClpB conformations in the presence of DnaK, identify a conserved TGIP loop linking the oligonucleotide/oligosaccharide-binding domain and the nucleotide-binding domain that is important for ClpB function, derive the interface between the regulatory middle domain of the ClpB and the DnaK nucleotide-binding domain, and find that DnaK binding stabilizes, but does not bend or tilt, the ClpB middle domain. We propose a model for the synergistic actions of aggregate dissolution and refolding by the Mtb ClpB-DnaK bi-chaperone system.
Identifiants
pubmed: 34038719
pii: S2211-1247(21)00508-8
doi: 10.1016/j.celrep.2021.109166
pmc: PMC8209680
mid: NIHMS1708604
pii:
doi:
Substances chimiques
Bacterial Proteins
0
Escherichia coli Proteins
0
Endopeptidase Clp
EC 3.4.21.92
Types de publication
Journal Article
Research Support, N.I.H., Extramural
Langues
eng
Sous-ensembles de citation
IM
Pagination
109166Subventions
Organisme : NCI NIH HHS
ID : P30 CA008748
Pays : United States
Organisme : NIAID NIH HHS
ID : R01 AI070285
Pays : United States
Organisme : NIAID NIH HHS
ID : U19 AI111143
Pays : United States
Informations de copyright
Copyright © 2021 The Author(s). Published by Elsevier Inc. All rights reserved.
Déclaration de conflit d'intérêts
Declaration of interests M.S.G. has received consulting fees and equity from Vedanta Biosciences and consulting fees from Takeda.
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