biostudies-literatureUnknown11Poonsiri TSiderophore-mediated iron acquisition is essential for the virulence of <i>Aspergillus fumigatus</i>, a fungus causing life-threatening aspergillosis. Drugs targeting the siderophore biosynthetic pathway could help improve disease management. The transacetylases SidF and SidL generate intermediates for different siderophores in <i>A. fumigatus</i>. <i>A. fumigatus</i> has a yet unidentified transacetylase that complements SidL during iron deficiency in SidL-lacking mutants. We present the first X-ray structure of SidF, revealing a two-domain architecture with tetrameric assembly. The N-terminal domain contributes to protein solubility and oligomerization, while the C-terminal domain containing the GCN5-related N-acetyltransferase (GNAT) motif is crucial for the enzymatic activity and mediaJournal of structural biology: X100119https://www.ebi.ac.uk/biostudies/studies/S-EPMC11751504biostudies-literatureSidF, a dual substrate N5-acetyl-N5-hydroxy-L-ornithine transacetylase involved in <i>Aspergillus fumigatus</i> siderophore biosynthesis.PMC11751504Haas HPoonsiri TCianci MDemitri NStransky JBenini SfalseSidF, a dual substrate N5-acetyl-N5-hydroxy-L-ornithine transacetylase involved in <i>Aspergillus fumigatus</i> siderophore biosynthesis.Siderophore-mediated iron acquisition is essential for the virulence of <i>Aspergillus fumigatus</i>, a fungus causing life-threatening aspergillosis. Drugs targeting the siderophore biosynthetic pathway could help improve disease management. The transacetylases SidF and SidL generate intermediates for different siderophores in <i>A. fumigatus</i>. <i>A. fumigatus</i> has a yet unidentified transacetylase that complements SidL during iron deficiency in SidL-lacking mutants. We present the first X-ray structure of SidF, revealing a two-domain architecture with tetrameric assembly. The N-terminal domain contributes to protein solubility and oligomerization, while the C-terminal domain containing the GCN5-related N-acetyltransferase (GNAT) motif is crucial for the enzymatic activity and media2025-01-01T00:00:00Z2025 Jun2026-06-02T20:50:02.005Z2025-04-05T11:34:33.39ZS-EPMC117515043984517310.1016/j.yjsbx.2024.100119