ArticleProceedings of the National Academy of Sciences of the United States of America2015
Crystal structure of the human mitochondrial chaperonin symmetrical football complex.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 71 papers.
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Who cites it
71 citing papers in PubMed.
- The mitochondrial chaperone HSPD1 folds MTHFD2 independently of its co-chaperone HSPE1.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2026Article
- Hsp10: From Single to Double Rings-Structural Basis of Protein Homeostasis.bioRxiv : the preprint server for biology · 2026Article
- Structural remodeling of the mitochondrial protein biogenesis machinery under proteostatic stress.Science advances · 2026Article
- When mitochondria lose their fold: matrix proteostasis and stress signaling.Frontiers in physiology · 2026Review
- Article
- Efficient production of human mitochondrial chaperonin (Hsp60/Hsp10) in Escherichia coli using a polyprotein strategy.Protein expression and purification · 2025Article
- In situ characterization of mitochondrial Hsp60-Hsp10 chaperone complex under folding stress.Science advances · 2025Article
- Role of heat shock proteins in renal function and adaptation to heat stress: Implications for global warming.World journal of nephrology · 2025Review
- Native Top-Down Proteomics of Endogenous Protein Complexes Enabled by Online Two-Dimensional Liquid Chromatography.Analytical chemistry · 2025Article
- Trioxane-based MS-cleavable cross-linking mass spectrometry for profiling multimeric interactions of cellular networks.Nature communications · 2025Article
- Pathogenic mutation impairs functional dynamics of Hsp60 in mono- and oligomeric states.Nature communications · 2025Article
- Advances in the structures, mechanisms and targeting of molecular chaperones.Signal transduction and targeted therapy · 2025Review
- Targeted Analysis of Mitochondrial Protein Conformations and Interactions by Endogenous ROS-Triggered Cross-Linker Release.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2024Article
- Asymmetric apical domain states of mitochondrial Hsp60 coordinate substrate engagement and chaperonin assembly.Nature structural & molecular biology · 2024Article
- Heat shock proteins as hallmarks of cancer: insights from molecular mechanisms to therapeutic strategies.Journal of hematology & oncology · 2024Review
- Mizoribine Promotes Molecular Chaperone HSP60/HSP10 Complex Formation.International journal of molecular sciences · 2024Article
- Cryo-EM structure and molecular dynamic simulations explain the enhanced stability and ATP activity of the pathological chaperonin mutant.Structure (London, England : 1993) · 2024Article
- Article
- Crystal structures of dimeric and heptameric mtHsp60 reveal the mechanism of chaperonin inactivation.Life science alliance · 2023Article
- Ectopic CH60 mediates HAPLN1-induced cell survival signaling in multiple myeloma.Life science alliance · 2023Article
11 more citing papers are in PubMed but not listed here.
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Authors and funding
5 authors.
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No grant is acknowledged in the PubMed record.
Abstract
Human mitochondria harbor a single type I chaperonin system that is generally thought to function via a unique single-ring intermediate. To date, no crystal structure has been published for any mammalian type I chaperonin complex. In this study, we describe the crystal structure of a football-shaped, double-ring human mitochondrial chaperonin complex at 3.15 Å, which is a novel intermediate, likely representing the complex in an early stage of dissociation. Interestingly, the mitochondrial chaperonin was captured in a state that exhibits subunit asymmetry within the rings and nucleotide symmetry between the rings. Moreover, the chaperonin tetradecamers show a different interring subunit arrangement when compared to GroEL. Our findings suggest that the mitochondrial chaperonins use a mechanism that is distinct from the mechanism of the well-studied Escherichia coli system.
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