Structure, assembly and inhibition of the Toxoplasma gondii respiratory chain supercomplex.

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 III₂-IV supercomplex and of the drug target complex III₂. The supercomplex structure reveals how clade-specific subunits form an apicomplexan-conserved III₂-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 III₂-IV in electron transfer efficiency as suggested for mammals. Nevertheless, knockout analysis indicates that III₂-IV is critical for parasite fitness. The compl

SUBMITTER: MacLean AE 

PROVIDER: S-EPMC12350165 | biostudies-literature | 2025 Aug

REPOSITORIES: biostudies-literature