ArticleActa crystallographica. Section F, Structural biology communications2014
Crystallization and structure determination of a symmetrical 'football' complex of the mammalian mitochondrial Hsp60-Hsp10 chaperonins.
Article in Acta crystallographica. Section F, Structural biology communications, 2014. 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.
- A mitochondrial unfolded protein response inhibitor suppresses prostate cancer growth in mice via HSP60.The Journal of clinical investigation · 2022Article
- Conserved and divergent chaperoning effects of Hsp60/10 chaperonins on protein folding landscapes.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Function and Fiber-Type Specific Distribution of Hsp60 and αB-Crystallin in Skeletal Muscles: Role of Physical Exercise.Biology · 2021Review
- Complex Destabilization in the Mitochondrial Chaperonin Hsp60 Leads to Disease.Frontiers in molecular biosciences · 2020Review
- MitCHAP-60 and Hereditary Spastic Paraplegia SPG-13 Arise from an Inactive hsp60 Chaperonin that Fails to Fold the ATP Synthase β-Subunit.Scientific reports · 2019Article
- Review
- Heat Shock Proteins in Alzheimer's Disease: Role and Targeting.International journal of molecular sciences · 2018Review
- Single-Ring Intermediates Are Essential for Some Chaperonins.Frontiers in molecular biosciences · 2018Article
- Creating the Functional Single-Ring GroEL-GroES Chaperonin Systems via Modulating GroEL-GroES Interaction.Scientific reports · 2017Article
- The human mitochondrial Hsp60 in the APO conformation forms a stable tetradecameric complex.Cell cycle (Georgetown, Tex.) · 2017Article
- Chaperonin of Group I: Oligomeric Spectrum and Biochemical and Biological Implications.Frontiers in molecular biosciences · 2017Review
- Characterization and function analysis of Hsp60 and Hsp10 under different acute stresses in black tiger shrimp, Penaeus monodon.Cell stress & chaperones · 2016Article
- Crystal structure of the human mitochondrial chaperonin symmetrical football complex.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Article
Corrections and comments
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Authors and funding
5 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The mitochondrial Hsp60-Hsp10 complex assists the folding of various proteins impelled by ATP hydrolysis, similar to the bacterial chaperonins GroEL and GroES. The near-atomic structural details of the mitochondrial chaperonins are not known, despite the fact that almost two decades have passed since the structures of the bacterial chaperonins became available. Here, the crystallization procedure, diffraction experiments and structure determination by molecular replacement of the mammalian mitochondrial chaperonin HSP60 (E321K mutant) and its co-chaperonin Hsp10 are reported.
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