{"doi":"10.1074/jbc.m406795200","title":"BeF  Stops the Chaperonin Cycle of GroEL-GroES and Generates a Complex with Double Folding Chambers","abstract":null,"journal":"Journal of Biological Chemistry","year":2004,"id":615583,"datarank":0.5955437870328184,"base_score":3.970291913552122,"endowment":3.970291913552122,"self_citation_contribution":0.5955437870328184,"citation_network_contribution":0.0,"self_endowment_contribution":0.5955437870328184,"citer_contribution":0.0,"corpus_percentile":null,"corpus_rank":null,"citation_count":52,"citer_count":0,"citers_with_citation_signal":0,"citers_with_endowment":0,"datacite_reuse_total":0,"is_dataset":false,"is_dataset_confidence":null,"is_data_producer":false,"deposit_databanks":null,"is_oa":false,"file_count":0,"downloads":0,"has_version_chain":false,"published_date":null,"fair_score":null,"fair_percentile":null,"algorithm_id":"datarank_citation_only_1hop_v6","ranking_scope":"data_only","authors":[{"id":1586773,"name":"Keigo Tsukuda","orcid":null,"position":1,"is_corresponding":false},{"id":146920,"name":"Fumihiro Motojima","orcid":"0000-0003-4461-8673","position":2,"is_corresponding":false},{"id":1561309,"name":"Ayumi Koike-Takeshita","orcid":null,"position":3,"is_corresponding":false},{"id":146926,"name":"Masasuke Yoshida","orcid":null,"position":4,"is_corresponding":false},{"id":587065,"name":"Hideki Taguchi","orcid":"0000-0002-6612-9339","position":0,"is_corresponding":false}],"reference_count":0,"raw_metadata":{"has_enrichment":true,"resolved":true,"title":"BeF  Stops the Chaperonin Cycle of GroEL-GroES and Generates a Complex with Double Folding Chambers","abstract":"Coupling with ATP hydrolysis and cooperating with GroES, the double ring chaperonin GroEL assists the folding of other proteins. Here we report novel GroEL-GroES complexes formed in fluoroberyllate (BeF(x)) that can mimic the phosphate part of the enzyme-bound nucleotides. In ATP, BeF(x) stops the functional turnover of GroEL by preventing GroES release and produces a symmetric 1:2 GroEL-GroES complex in which both GroEL rings contain ADP.BeF(x) and an encapsulated substrate protein. In ADP, the substrate protein-loaded GroEL cannot bind GroES. In ADP plus BeF(x), however, it can bind GroES to form a stable 1:1 GroEL-GroES complex in which one of GroEL rings contains ADP.BeF(x) and an encapsulated substrate protein. This 1:1 GroEL-GroES complex is converted into the symmetric 1:2 GroEL-GroES complex when GroES is supplied in ATP plus BeF(x). Thus, BeF(x) stabilizes two GroEL-GroES complexes; one with a single folding chamber and the other with double folding chambers. These results shed light on the intermediate ADP.P(i) nucleotide states in the functional cycle of GroEL.","is_dataset_classified":null,"base_score":3.970291913552122,"endowment":3.970291913552122,"datacite_reuse_total":0,"file_count":0,"downloads":0,"views":0,"has_version_chain":false,"is_dataset":false,"is_oa":false,"pmid":"15347650","pmcid":null,"openalex_id":"https://openalex.org/W1986382489","authors":[],"funders":[],"total_grants":0,"fwci":1.1337,"citation_percentile":0.74516661,"influential_citations":0,"citation_trend":[{"year":2012,"count":2},{"year":2013,"count":2},{"year":2014,"count":4},{"year":2015,"count":5},{"year":2016,"count":3},{"year":2017,"count":2},{"year":2018,"count":1},{"year":2020,"count":3},{"year":2021,"count":2},{"year":2022,"count":1},{"year":2023,"count":1},{"year":2024,"count":6},{"year":2025,"count":1}],"oa_status":"hybrid","license":"cc-by","oa_locations":[{"url":"https://doi.org/10.1074/jbc.m406795200","host_type":"journal"},{"url":"https://doi.org/10.1074/jbc.m406795200","host_type":"publisher"},{"url":"https://api.elsevier.com/content/article/PII:S002192582072507X?httpAccept=text/xml","host_type":"publisher"},{"url":"https://api.elsevier.com/content/article/PII:S002192582072507X?httpAccept=text/plain","host_type":"publisher"},{"url":"https://syndication.highwire.org/content/doi/10.1074/jbc.M406795200","host_type":"publisher"},{"url":"https://pubmed.ncbi.nlm.nih.gov/15347650","host_type":"repository"},{"url":"http://www.jbc.org/article/S002192582072507X/pdf","host_type":"Unpaywall"}],"fields_of_study":["Heat shock proteins research","Enzyme Structure and Function","Protein Structure and Dynamics","Adenosine Triphosphate","Beryllium","Chaperonin 10","Chaperonin 60","Fluorides","Hydrolysis","Protein Folding"],"mesh_terms":["Adenosine Triphosphate","Beryllium","Fluorides","Hydrolysis","Protein Folding","Chaperonin 60","Chaperonin 10"],"keywords":["GroEL","GroES","Chaperonin","Foldase","Protein folding","ATP hydrolysis","Chaperone (clinical)","Folding (DSP implementation)","Biophysics","Biochemistry","Crystallography","Chemistry","Biology","Enzyme","Escherichia coli"],"sdg_mappings":[],"linked_datasets":[],"clinical_trials":[],"software_tools":[],"database_accessions":[],"source":"live","citation_network_status":"fetched"},"created_at":"2026-08-02T20:27:39.723700Z","pmid":null,"pmcid":null,"fwci":null,"citation_percentile":null,"influential_citations":0,"oa_status":null,"license":null,"views":0,"total_file_size_bytes":0,"version_count":0,"fair_f":null,"fair_a":null,"fair_i":null,"fair_r":null,"fair_zscore":null,"fair_rationale":null,"fair_model":null,"fair_agent_version":null,"fair_fulltext_source":null,"fair_has_llm":null,"fair_computed_at":null,"clinical_trials":[],"software_tools":[],"db_accessions":[],"linked_datasets":[],"topics":[]}