{"doi":"10.1074/jbc.m114.593822","title":"Asp-52 in Combination with Asp-398 Plays a Critical Role in ATP Hydrolysis of Chaperonin GroEL","abstract":null,"journal":"Journal of Biological Chemistry","year":2014,"id":607991,"datarank":0.4335557636844247,"base_score":2.8903717578961645,"endowment":2.8903717578961645,"self_citation_contribution":0.4335557636844247,"citation_network_contribution":0.0,"self_endowment_contribution":0.4335557636844247,"citer_contribution":0.0,"corpus_percentile":null,"corpus_rank":null,"citation_count":17,"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":1484055,"name":"Kaoru Mitsuoka","orcid":"0000-0003-1782-675X","position":1,"is_corresponding":false},{"id":587065,"name":"Hideki Taguchi","orcid":"0000-0002-6612-9339","position":2,"is_corresponding":false},{"id":1561309,"name":"Ayumi Koike-Takeshita","orcid":null,"position":0,"is_corresponding":false}],"reference_count":0,"raw_metadata":{"has_enrichment":true,"resolved":true,"title":"Asp-52 in Combination with Asp-398 Plays a Critical Role in ATP Hydrolysis of Chaperonin GroEL","abstract":"The Escherichia coli chaperonin GroEL is a double-ring chaperone that assists protein folding with the aid of GroES and ATP. Asp-398 in GroEL is known as one of the critical residues on ATP hydrolysis because GroEL(D398A) mutant is deficient in ATP hydrolysis (<2% of the wild type) but not in ATP binding. In the archaeal Group II chaperonin, another aspartate residue, Asp-52 in the corresponding E. coli GroEL, in addition to Asp-398 is also important for ATP hydrolysis. We investigated the role of Asp-52 in GroEL and found that ATPase activity of GroEL(D52A) and GroEL(D52A/D398A) mutants was ∼ 20% and <0.01% of wild-type GroEL, respectively, indicating that Asp-52 in E. coli GroEL is also involved in the ATP hydrolysis. GroEL(D52A/D398A) formed a symmetric football-shaped GroEL-GroES complex in the presence of ATP, again confirming the importance of the symmetric complex during the GroEL ATPase cycle. Notably, the symmetric complex of GroEL(D52A/D398A) was extremely stable, with a half-time of ∼ 150 h (∼ 6 days), providing a good model to characterize the football-shaped complex.","is_dataset_classified":null,"base_score":2.8903717578961645,"endowment":2.8903717578961645,"datacite_reuse_total":0,"file_count":0,"downloads":0,"views":0,"has_version_chain":false,"is_dataset":false,"is_oa":false,"pmid":"25202010","pmcid":null,"openalex_id":"https://openalex.org/W2056842319","authors":[],"funders":[],"total_grants":0,"fwci":0.7799,"citation_percentile":0.70173589,"influential_citations":0,"citation_trend":[{"year":2014,"count":1},{"year":2015,"count":3},{"year":2016,"count":2},{"year":2018,"count":1},{"year":2019,"count":1},{"year":2020,"count":1},{"year":2023,"count":3},{"year":2024,"count":2},{"year":2025,"count":3}],"oa_status":"hybrid","license":"cc-by","oa_locations":[{"url":"http://www.jbc.org/article/S0021925820373336/pdf","host_type":"journal"},{"url":"http://www.jbc.org/article/S0021925820373336/pdf","host_type":"publisher"},{"url":"https://api.elsevier.com/content/article/PII:S0021925820373336?httpAccept=text/xml","host_type":"publisher"},{"url":"https://api.elsevier.com/content/article/PII:S0021925820373336?httpAccept=text/plain","host_type":"publisher"},{"url":"https://syndication.highwire.org/content/doi/10.1074/jbc.M114.593822","host_type":"publisher"},{"url":"https://doi.org/10.1074/jbc.m114.593822","host_type":"journal"},{"url":"https://pubmed.ncbi.nlm.nih.gov/25202010","host_type":"repository"},{"url":"https://www.ncbi.nlm.nih.gov/pmc/articles/4208008","host_type":"repository"},{"url":"http://t2r2.star.titech.ac.jp/cgi-bin/publicationinfo.cgi?q_publication_content_number=CTT100785693","host_type":"repository"}],"fields_of_study":["Heat shock proteins research","Enzyme Structure and Function","Protein Structure and Dynamics"],"mesh_terms":["Adenosine Triphosphate","Aspartic Acid","Binding Sites","Escherichia coli","Hydrolysis","Malate Dehydrogenase","Structure-Activity Relationship","Thiosulfate Sulfurtransferase","Negative Staining","Protein Folding","Chaperonin 60","Chaperonin 10","Protein Subunits","Mutant Proteins","Protein Stability"],"keywords":["GroEL","GroES","Chaperonin","ATP hydrolysis","Foldase","Chaperone (clinical)","Biochemistry","Mutant","Protein folding","ATPase","Hydrolysis","Escherichia coli","Biology","Chemistry","Enzyme","Medicine","Gene"],"sdg_mappings":[],"linked_datasets":[],"clinical_trials":[],"software_tools":[],"database_accessions":[],"source":"live","citation_network_status":"fetched"},"created_at":"2026-07-30T07:19:58.495876Z","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":[]}