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TitleMolecular insights into fungal inositol phosphorylceramide synthesis and its inhibition by antifungal aureobasidin A.
Journal, issue, pagesNat Commun, Year 2026
Publish dateFeb 19, 2026
AuthorsJiehui Chen / Yan Ke / Min Zhang / Xinyuan Lin / Zhengkang Hua / Di Zhang / Xinlin Hu / Xuyang Ding / Jiameng Li / Ping Yang / Hongjun Yu /
PubMed AbstractFungal inositol phosphorylceramide (IPC) synthase is an essential enzyme complex that catalyzes a critical step in sphingolipid biosynthesis. It is the molecular target of potent antifungal ...Fungal inositol phosphorylceramide (IPC) synthase is an essential enzyme complex that catalyzes a critical step in sphingolipid biosynthesis. It is the molecular target of potent antifungal aureobasidin A (AbA). Despite its therapeutic relevance, the lack of structural and mechanistic insights into IPC synthase function and inhibition has impeded rational antifungal drug development. Here, we present cryo-EM structures of Saccharomyces cerevisiae IPC synthase in two distinct functional states: a ceramide-bound form and an AbA-inhibited complex. Our study reveals a conserved heterodimeric architecture formed by Aur1 and Kei1, stabilized through extensive protein-protein and lipid-mediated interactions. Within catalytic Aur1, we identify a membrane-embedded reaction chamber harboring a conserved H-H-D catalytic triad (H255, H294, and D298) essential for IPC synthesis. Structural comparisons illuminate the mechanism of ceramide recognition and reveal how AbA acts as a competitive inhibitor by occupying the substrate-binding pocket. Further analyses identify key residues involved in AbA binding and explain the molecular basis of drug resistance. Together, these findings advance the mechanistic understanding of fungal IPC biosynthesis and inhibition, and establish a foundation for developing new antifungal drugs targeting IPC synthase.
External linksNat Commun / PubMed:41708645
MethodsEM (single particle)
Resolution3.5 - 3.53 Å
Structure data

65103

9vj4

EMDB-65103, PDB-9vj4:
Structure of a membrane-bound inositol phosphorylceramide synthase and ceramide complex
Method: EM (single particle) / Resolution: 3.5 Å

66750

9xd0

EMDB-66750, PDB-9xd0:
Structure of a membrane-bound inositol phosphorylceramide synthase and Aureobasidin A complex
Method: EM (single particle) / Resolution: 3.53 Å

Chemicals


ChemComp, No image

ChemComp-UJO:
Unknown entry

ChemComp-C14:
TETRADECANE

ChemComp-46E:
(2R)-3-{[(S)-(2-aminoethoxy)(hydroxy)phosphoryl]oxy}-2-(tetradecanoyloxy)propyl tetradecanoate

Source
  • Saccharomyces cerevisiae (brewer's yeast)
  • saccharomyces cerevisiae s288c (yeast)
  • synthetic construct (others)
KeywordsLIPID BINDING PROTEIN / membrane protein / inositol phosphorylceramide synthase / TRANSFERASE

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