ArticleStructure (London, England : 1993)2016
Ring Separation Highlights the Protein-Folding Mechanism Used by the Phage EL-Encoded Chaperonin.
Article in Structure (London, England : 1993), 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 20 citations in OpenAlex.
- Protein Quality Control is a Master Modulator of Molecular Evolution in Bacteria.Genome biology and evolution · 2025Review
- Proteostasis in Viral Infection: Unfolding the Complex Virus-Chaperone Interplay.Cold Spring Harbor perspectives in biology · 2020Review
- Article
- 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
- Single-Ring Intermediates Are Essential for Some Chaperonins.Frontiers in molecular biosciences · 2018Article
- The human mitochondrial Hsp60 in the APO conformation forms a stable tetradecameric complex.Cell cycle (Georgetown, Tex.) · 2017Article
- Dynamic Complexes in the Chaperonin-Mediated Protein Folding Cycle.Frontiers in molecular biosciences · 2016Review
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Authors and funding
11 authors at 7 institutions in 2 countries.
Funding
Abstract
Chaperonins are ubiquitous, ATP-dependent protein-folding molecular machines that are essential for all forms of life. Bacteriophage φEL encodes its own chaperonin to presumably fold exceedingly large viral proteins via profoundly different nucleotide-binding conformations. Our structural investigations indicate that ATP likely binds to both rings simultaneously and that a misfolded substrate acts as the trigger for ATP hydrolysis. More importantly, the φEL complex dissociates into two single rings resulting from an evolutionarily altered residue in the highly conserved ATP-binding pocket. Conformational changes also more than double the volume of the single-ring internal chamber such that larger viral proteins are accommodated. This is illustrated by the fact that φEL is capable of folding β-galactosidase, a 116-kDa protein. Collectively, the architecture and protein-folding mechanism of the φEL chaperonin are significantly different from those observed in group I and II chaperonins.
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