{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["MacLean AE"],"funding":["BLRD VA","NIAID NIH HHS","Wellcome Trust"],"pagination":["1424-1433"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC12350165"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["32(8)"],"pubmed_abstract":["The apicomplexan mitochondrial electron transport chain is essential for parasite survival and displays a divergent subunit composition. Here we report cryo-electron microscopy structures of an apicomplexan III<sub>2</sub>-IV supercomplex and of the drug target complex III<sub>2</sub>. The supercomplex structure reveals how clade-specific subunits form an apicomplexan-conserved III<sub>2</sub>-IV interface with a unique, kinked architecture, suggesting that supercomplexes evolved independently in different eukaryotic lineages. A knockout resulting in supercomplex disassembly challenges the proposed role of III<sub>2</sub>-IV in electron transfer efficiency as suggested for mammals. Nevertheless, knockout analysis indicates that III<sub>2</sub>-IV is critical for parasite fitness. The compl"],"journal":["Nature structural & molecular biology"],"pubmed_title":["Structure, assembly and inhibition of the Toxoplasma gondii respiratory chain supercomplex."],"pmcid":["PMC12350165"],"funding_grant_id":["I01 BX003312","I01 BX004522","IK6 BX004857","R01 AI141412","104111","097945/B/11/Z","R01 AI100569"],"pubmed_authors":["Liebman KM","Winter RW","Sheiner L","Meir A","Shikha S","Riscoe MK","Pou S","Muhleip A","Nilsen A","Doggett JS","Ferreira Silva M","Gramelspacher MJ","MacLean AE"],"additional_accession":[]},"is_claimable":false,"name":"Structure, assembly and inhibition of the Toxoplasma gondii respiratory chain supercomplex.","description":"The apicomplexan mitochondrial electron transport chain is essential for parasite survival and displays a divergent subunit composition. Here we report cryo-electron microscopy structures of an apicomplexan III<sub>2</sub>-IV supercomplex and of the drug target complex III<sub>2</sub>. The supercomplex structure reveals how clade-specific subunits form an apicomplexan-conserved III<sub>2</sub>-IV interface with a unique, kinked architecture, suggesting that supercomplexes evolved independently in different eukaryotic lineages. A knockout resulting in supercomplex disassembly challenges the proposed role of III<sub>2</sub>-IV in electron transfer efficiency as suggested for mammals. Nevertheless, knockout analysis indicates that III<sub>2</sub>-IV is critical for parasite fitness. The compl","dates":{"release":"2025-01-01T00:00:00Z","publication":"2025 Aug","modification":"2026-05-29T17:34:32.111Z","creation":"2026-04-08T05:36:54.927Z"},"accession":"S-EPMC12350165","cross_references":{"pubmed":["40389671"],"doi":["10.1038/s41594-025-01531-7"]}}