{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Syed A"],"funding":["NIAID NIH HHS","National Natural Science Foundation of China","NIH","NIH Common Fund","NIGMS NIH HHS"],"pagination":["575-584.e3"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC11069440"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["32(5)"],"pubmed_abstract":["Chaperonins Hsp60s are required for cellular vitality by assisting protein folding in an ATP-dependent mechanism. Although conserved, the human mitochondrial mHsp60 exhibits molecular characteristics distinct from the E. coli GroEL, with different conformational assembly and higher subunit association dynamics, suggesting a different mechanism. We previously found that the pathological mutant mHsp60<sup>V72I</sup> exhibits enhanced subunit association stability and ATPase activity. To provide structural explanations for the V72I mutational effects, here we determined a cryo-EM structure of mHsp60<sup>V72I</sup>. Our structural analysis combined with molecular dynamic simulations showed mHsp60<sup>V72I</sup> with increased inter-subunit interface, binding free energy, and dissociation force"],"journal":["Structure (London, England : 1993)"],"pubmed_title":["Cryo-EM structure and molecular dynamic simulations explain the enhanced stability and ATP activity of the pathological chaperonin mutant."],"pmcid":["PMC11069440"],"funding_grant_id":["U24 GM129539","R01 AI173104"],"pubmed_authors":["Wang JC","Chen L","Zhai J","Syed A","Guo B","Zhao Y"],"additional_accession":[]},"is_claimable":false,"name":"Cryo-EM structure and molecular dynamic simulations explain the enhanced stability and ATP activity of the pathological chaperonin mutant.","description":"Chaperonins Hsp60s are required for cellular vitality by assisting protein folding in an ATP-dependent mechanism. Although conserved, the human mitochondrial mHsp60 exhibits molecular characteristics distinct from the E. coli GroEL, with different conformational assembly and higher subunit association dynamics, suggesting a different mechanism. We previously found that the pathological mutant mHsp60<sup>V72I</sup> exhibits enhanced subunit association stability and ATPase activity. To provide structural explanations for the V72I mutational effects, here we determined a cryo-EM structure of mHsp60<sup>V72I</sup>. Our structural analysis combined with molecular dynamic simulations showed mHsp60<sup>V72I</sup> with increased inter-subunit interface, binding free energy, and dissociation force","dates":{"release":"2024-01-01T00:00:00Z","publication":"2024 May","modification":"2026-06-02T20:56:11.511Z","creation":"2025-07-06T03:05:51.298Z"},"accession":"S-EPMC11069440","cross_references":{"pubmed":["38412855"],"doi":["10.1016/j.str.2024.02.001"]}}