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MechanismsofaureobasidinA inhibition and drug resistance in a fungal IPC synthase complex

nature COMMUNICATION. 2025-05; 
Xinyue Wu , Xin Gong , Tian Xie
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Proteins, Expression, Isolation and Analysis After centrifugation at 37,000 g for 30 minutes at 4 °C, the supernatant was collected and incubated with Strep-Tactin affinity resin (IBA, Cat# 2-5010-010) or anti-Flag G1 affinity resin (GenScript, Cat# L00432) for 1 hour at 4 °C. Get A Quote

摘要

The enzyme inositol phosphorylceramide (IPC) synthase is essential for survival and virulence in fungi, while absent in mammals, thus representing a potential target for antifungal treatments. Aureobasidin A (AbA), a natural cyclic peptide, displays antifungal activity and inhibits IPC synthase, but the precise molecular mechanism remains unclear. Here, we present the cryo-EM structure of the Saccharomyces cerevisiae IPC synthase, composed of catalytic subunit Aur1 and regulatory subunit Kei1, in its AbA-bound state. The complex is resolved as a dimer of Aur1-Kei1 heterodimers, with Aur1 mediating homodimerization. AbA occupies a predominantly hydrophobic pocket in the catalytic core domain of each Aur1 subunit... More

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