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9QDM

CRYO-EM STRUCTURE OF THE YEAST RESPIRATORY COMPLEX II WITH THE INHIBITOR BIXAFEN

This is a non-PDB format compatible entry.
Summary for 9QDM
Entry DOI10.2210/pdb9qdm/pdb
EMDB information53030
DescriptorSuccinate dehydrogenase [ubiquinone] flavoprotein subunit, mitochondrial, bixafen, 1,2-Distearoyl-sn-glycerophosphoethanolamine, ... (12 entities in total)
Functional Keywordscomplex ii, membrane protein, oxidoreductase, oxidoreductase inhibitor complex, bixafen
Biological sourceSaccharomyces cerevisiae (brewer's yeast)
More
Total number of polymer chains4
Total formula weight147810.54
Authors
Pinotsis, N.,Marechal, A.,Berry, E.A.,Shu, C. (deposition date: 2025-03-06, release date: 2026-02-11, Last modification date: 2026-02-18)
Primary citationPinotsis, N.,Burn-Leefe, C.,Jones, S.,Chen, S.,Lukoyanova, N.,Meunier, B.,Berry, E.A.,Marechal, A.
Cryo-EM structure of bixafen-bound S. cerevisiae complex II unravels SDHI specificity against pathogenic fungi.
Commun Biol, 2026
Cited by
PubMed Abstract: Respiratory complex II (CII), or succinate dehydrogenase, couples succinate oxidation in the Krebs cycle with electron transfer to the respiratory chain. Owing to this pivotal role, CII inhibitors are widely used fungicides globally; however, their development has largely proceeded without structural insights from fungal targets. Here, we report cryo-electron microscopy structures of the 128 kDa mitochondrial CII from Saccharomyces cerevisiae in two states: active, with endogenous ubiquinone-6 bound (3.15 Å), and inhibited with the fungicide bixafen (3.00 Å). Although closely related to the mammalian type C enzyme, our structures show that the yeast CII has lost the canonical heme cofactor. They also reveal how clade-specific sequence extensions of the membrane subunits Sdh3 and Sdh4 - conserved in pathogenic fungi - uniquely contribute to complex stability and fungicide binding. Our findings provide a foundation for rational design of next-generation CII inhibitors and combatting resistance, in both agriculture and human health.
PubMed: 41606097
DOI: 10.1038/s42003-026-09617-8
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3 Å)
Structure validation

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