ArticleCell reports2021
Structural basis for aggregate dissolution and refolding by the Mycobacterium tuberculosis ClpB-DnaK bi-chaperone system.
Article in Cell reports, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 31 citations in OpenAlex.
- A Pilot Proteomics Analysis ofInternational journal of molecular sciences · 2026Article
- Expanding the CarD interaction network: CrsL is a novel transcription regulator in actinobacteria.Nucleic acids research · 2025Article
- A split ALFA tag-nanobody system for protein localization and proximity proteomics in mycobacteria.mBio · 2025Article
- Hsp90, DnaK, and ClpB collaborate in protein reactivation.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Design principles to tailor Hsp104 therapeutics.Cell reports · 2024Article
- Unmasking AlphaFold to integrate experiments and predictions in multimeric complexes.Nature communications · 2024Article
- Design principles to tailor Hsp104 therapeutics.bioRxiv : the preprint server for biology · 2024Article
- HtpG-A Major Virulence Factor and a Promising Vaccine Antigen againstBiomolecules · 2024Review
- Structure of the M. tuberculosis DnaK-GrpE complex reveals how key DnaK roles are controlled.Nature communications · 2024Article
- CLPB3 is required for the removal of chloroplast protein aggregates and thermotolerance in Chlamydomonas.Journal of experimental botany · 2023Article
- Automatic and accurate ligand structure determination guided by cryo-electron microscopy maps.Nature communications · 2023Article
- Electron microscopy holdings of the Protein Data Bank: the impact of the resolution revolution, new validation tools, and implications for the future.Biophysical reviews · 2022Review
- AAA+ proteins: one motor, multiple ways to work.Biochemical Society transactions · 2022Review
- Multi-Omics Profiling Specifies Involvement of Alternative Ribosomal Proteins in Response to Zinc Limitation inFrontiers in microbiology · 2022Article
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
Abstract
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.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.