ArticleProceedings of the National Academy of Sciences of the United States of America2014
Formation and structures of GroEL:GroES2 chaperonin footballs, the protein-folding functional form.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.
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Who cites it
45 citing papers in PubMed.
- Roles of Hydration in Protein-Ligand Binding: Passive or Active Participant?The journal of physical chemistry. A · 2025Article
- Allostery without Conformational Change: A Native Mass Spectrometry Perspective.The journal of physical chemistry. B · 2025Article
- Asymmetric apical domain states of mitochondrial Hsp60 coordinate substrate engagement and chaperonin assembly.Nature structural & molecular biology · 2024Article
- Article
- Synonymous and non-synonymous codon substitutions can alleviate dependence on GroEL for folding.Protein science : a publication of the Protein Society · 2024Article
- Native Capillary Electrophoresis-Mass Spectrometry of Near 1 MDa Non-Covalent GroEL/GroES/Substrate Protein Complexes.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2024Article
- A diminished hydrophobic effect inside the GroEL/ES cavity contributes to protein substrate destabilization.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Cryo-EM structures of GroEL:ESiScience · 2022Article
- Supramolecular assembly of protein building blocks: from folding to function.Nano convergence · 2022Review
- The Functional Differences between the GroEL Chaperonin ofBiomolecules · 2021Article
- Visualization of Sparsely-populated Lower-order Oligomeric States of Human Mitochondrial Hsp60 by Cryo-electron Microscopy.Journal of molecular biology · 2021Article
- Novel cryo-EM structure of an ADP-bound GroEL-GroES complex.Scientific reports · 2021Article
- Reliable identification of protein-protein interactions by crosslinking mass spectrometry.Nature communications · 2021Article
- Crystal structure of P. falciparum Cpn60 bound to ATP reveals an open dynamic conformation before substrate binding.Scientific reports · 2021Article
- Retardation of Folding Rates of Substrate Proteins in the Nanocage of GroEL.Biochemistry · 2021Article
- First-Principles Collision Cross Section Measurements of Large Proteins and Protein Complexes.Analytical chemistry · 2020Article
- OsCpn60β1 is Essential for Chloroplast Development in Rice (International journal of molecular sciences · 2020Article
- Structural basis for active single and double ring complexes in human mitochondrial Hsp60-Hsp10 chaperonin.Nature communications · 2020Article
- Iterative annealing mechanism explains the functions of the GroEL and RNA chaperones.Protein science : a publication of the Protein Society · 2020Review
- Missense Mutations of Human Hsp60: A Computational Analysis to Unveil Their Pathological Significance.Frontiers in genetics · 2020Article
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4 authors.
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Abstract
The GroE chaperonins assist substrate protein (SP) folding by cycling through several conformational states. With each cycle the SP is, in turn, captured, unfolded, briefly encapsulated (t1/2 ∼ 1 s), and released by the chaperonin complex. The protein-folding functional form is the US-football-shaped GroEL:GroES2 complex. We report structures of two such "football" complexes to ∼ 3.7-Å resolution; one is empty whereas the other contains encapsulated SP in both chambers. Although encapsulated SP is not visible on the electron density map, using calibrated FRET and order-of-addition experiments we show that owing to SP-catalyzed ADP/ATP exchange both chambers of the football complex encapsulate SP efficiently only if the binding of SP precedes that of ATP. The two rings of GroEL thus behave as a parallel processing machine, rather than functioning alternately. Compared with the bullet-shaped GroEL:GroES1 complex, the GroEL:GroES2 football complex differs conformationally at the GroEL-GroES interface and also at the interface between the two GroEL rings. We propose that the electrostatic interactions between the ε-NH(3+) of K105 of helix D in one ring with the negatively charged carboxyl oxygen of A109 at the carboxyl end of helix D of the other ring provide the structural basis for negative inter-ring cooperativity.
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