ArticleThe Journal of biological chemistry2010
Crystal structures of a group II chaperonin reveal the open and closed states associated with the protein folding cycle.
Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.
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Who cites it
41 citing papers in PubMed, 74 citations in OpenAlex.
- CryoEM Strategies for Elucidating the Closed State Architecture of CCT.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Structural Stability Comparisons Between Natural and Engineered Group II Chaperonins: Are Crenarchaeal "Heat Shock" Proteins Also "pH Shock" Resistant?Microorganisms · 2024Article
- Comparative Natural History of Visual Function From Patients With Biallelic Variants in BBS1 and BBS10.Investigative ophthalmology & visual science · 2021Article
- CryoEM reveals the stochastic nature of individual ATP binding events in a group II chaperonin.Nature communications · 2021Article
- Article
- Chaperonins: Nanocarriers with Biotechnological Applications.Nanomaterials (Basel, Switzerland) · 2021Review
- First-Principles Collision Cross Section Measurements of Large Proteins and Protein Complexes.Analytical chemistry · 2020Article
- An ensemble of cryo-EM structures of TRiC reveal its conformational landscape and subunit specificity.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Bridging human chaperonopathies and microbial chaperonins.Communications biology · 2019Review
- Structural investigation of a chaperonin in action reveals how nucleotide binding regulates the functional cycle.Science advances · 2018Article
- Intraring allostery controls the function and assembly of a hetero-oligomeric class II chaperonin.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2018Article
- Berkeley Screen: a set of 96 solutions for general macromolecular crystallization.Journal of applied crystallography · 2017Article
- An information theoretic framework reveals a tunable allosteric network in group II chaperonins.Nature structural & molecular biology · 2017Article
- Structure of the human TRiC/CCT Subunit 5 associated with hereditary sensory neuropathy.Scientific reports · 2017Article
- Asymmetry in the function and dynamics of the cytosolic group II chaperonin CCT/TRiC.PloS one · 2017Article
- Staggered ATP binding mechanism of eukaryotic chaperonin TRiC (CCT) revealed through high-resolution cryo-EM.Nature structural & molecular biology · 2016Article
- Replacement of GroEL in Escherichia coli by the Group II Chaperonin from the Archaeon Methanococcus maripaludis.Journal of bacteriology · 2016Article
- Structural biology in antiviral drug discovery.Current opinion in pharmacology · 2016Review
- Purification, crystallization, and preliminary X-ray crystallographic analysis of the Group III chaperonin from Carboxydothermus hydrogenoformans.Journal of microbiology (Seoul, Korea) · 2016Article
- Prokaryotic Chaperonins as Experimental Models for Elucidating Structure-Function Abnormalities of Human Pathogenic Mutant Counterparts.Frontiers in molecular biosciences · 2016Review
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Authors and funding
9 authors at 4 institutions in 1 country.
Funding
Abstract
Chaperonins are large protein complexes consisting of two stacked multisubunit rings, which open and close in an ATP-dependent manner to create a protected environment for protein folding. Here, we describe the first crystal structure of a group II chaperonin in an open conformation. We have obtained structures of the archaeal chaperonin from Methanococcus maripaludis in both a peptide acceptor (open) state and a protein folding (closed) state. In contrast with group I chaperonins, in which the equatorial domains share a similar conformation between the open and closed states and the largest motions occurs at the intermediate and apical domains, the three domains of the archaeal chaperonin subunit reorient as a single rigid body. The large rotation observed from the open state to the closed state results in a 65% decrease of the folding chamber volume and creates a highly hydrophilic surface inside the cage. These results suggest a completely distinct closing mechanism in the group II chaperonins as compared with the group I chaperonins.
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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.