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Structure paper

TitleStructure, assembly and inhibition of the Toxoplasma gondii respiratory chain supercomplex.
Journal, issue, pagesNat Struct Mol Biol, Year 2025
Publish dateMay 19, 2025
AuthorsAndrew E MacLean / Shikha Shikha / Mariana Ferreira Silva / Max J Gramelspacher / Aaron Nilsen / Katherine M Liebman / Sovitj Pou / Rolf W Winter / Amit Meir / Michael K Riscoe / J Stone Doggett / Lilach Sheiner / Alexander Mühleip /
PubMed AbstractThe 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 ...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-IV supercomplex and of the drug target complex III. The supercomplex structure reveals how clade-specific subunits form an apicomplexan-conserved III-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-IV in electron transfer efficiency as suggested for mammals. Nevertheless, knockout analysis indicates that III-IV is critical for parasite fitness. The complexes from the model parasite Toxoplasma gondii were inhibited with the antimalarial atovaquone, revealing interactions underpinning species specificity. They were also inhibited with endochin-like quinolone (ELQ)-300, an inhibitor in late-stage preclinical development. Notably, in the apicomplexan binding site, ELQ-300 is flipped compared with related compounds in the mammalian enzyme. On the basis of the binding modes and parasite-specific interactions discovered, we designed more potent ELQs with subnanomolar activity against T. gondii. Our findings reveal critical evolutionary differences in the role of supercomplexes in mitochondrial biology and provide insight into cytochrome b inhibition, informing future drug discovery.
External linksNat Struct Mol Biol / PubMed:40389671
MethodsEM (single particle)
Resolution1.8 - 2.67 Å
Structure data

51157

9g9t

EMDB-51157, PDB-9g9t:
Cryo-EM structure of the Toxoplasma gondii respiratory chain complex III inhibited by ELQ-300
Method: EM (single particle) / Resolution: 1.8 Å

51939

9h8t

EMDB-51939, PDB-9h8t:
Cryo-EM structure of the atovaquone-inhibited Complex III from the Chlorocebus sabaeus respirasome
Method: EM (single particle) / Resolution: 2.67 Å

Chemicals

ChemComp-CDL:
CARDIOLIPIN / phospholipid*YM

PDB-1ijd:
Crystallographic Structure of the LH3 Complex from Rhodopseudomonas acidophila strain 7050

ChemComp-HEM:
PROTOPORPHYRIN IX CONTAINING FE

ChemComp-MG:
Unknown entry

ChemComp-HEC:
HEME C

ChemComp-PC1:
1,2-DIACYL-SN-GLYCERO-3-PHOSPHOCHOLINE / phospholipid*YM

ChemComp-ZN:
Unknown entry

ChemComp-HOH:
WATER

ChemComp-FES:
FE2/S2 (INORGANIC) CLUSTER

ChemComp-AOQ:
2-[trans-4-(4-chlorophenyl)cyclohexyl]-3-hydroxynaphthalene-1,4-dione / medication, Antimicrobial*YM

ChemComp-PEE:
1,2-dioleoyl-sn-glycero-3-phosphoethanolamine / DOPE, phospholipid*YM

ChemComp-AFI:
2-[4-(4-CHLOROPHENYL)CYCLOHEXYLIDENE]-3,4-DIHYDROXY-1(2H)-NAPHTHALENONE

Source
  • toxoplasma gondii (eukaryote)
  • chlorocebus sabaeus (green monkey)
KeywordsELECTRON TRANSPORT / cytochrome bc1 complex / complex III / respiratory chain / respirasome / mitochondria / green african monkey / atovaquone

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