Fig. 3: Conformational change and lipid environment remodeling of FKS by Enfumafungin.
From: Inhibition mechanism of the fungal β−1,3-glucan synthases by triterpenoid antifungal drugs
a Structural comparison between Fks1–EFU (blue), Fks1–apo (gray) and Fks2-EFU (green). b Zoom in view of the EFU binding site in panel (a). c Ordered lipid densities around EFU, TM8 linker, and HH2B in cryo-EM maps of Fks1–EFU–Lip and Fks2–EFU–Lip. d Interaction network between ordered ergosterols and Fks1. Key residues involved in the interaction are shown as sticks. e Mapping of reported ibrexafungerp-resistant mutations in Fks1–EFU structure. The Cα atoms of ibrexafungerp-resistant mutations summarized in Supplementary Table 2 are shown as salmon spheres. f Growth complementation of fks1Δ cells with empty plasmid (fks1Δ), or plasmid carrying either WT Fks1 (FKS1) or mutants. Cells were serially diluted, spotted onto synthetic Histidine-dropout medium plates (SD-His) and SD-His plates with 0.1 μg/mL FK506, and incubated at 30 °C for 2 days. Source data are provided as a Source Data file.
