{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["11"],"submitter":["Poonsiri T"],"pubmed_abstract":["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 media"],"journal":["Journal of structural biology: X"],"pagination":["100119"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC11751504"],"repository":["biostudies-literature"],"pubmed_title":["SidF, a dual substrate N5-acetyl-N5-hydroxy-L-ornithine transacetylase involved in <i>Aspergillus fumigatus</i> siderophore biosynthesis."],"pmcid":["PMC11751504"],"pubmed_authors":["Haas H","Poonsiri T","Cianci M","Demitri N","Stransky J","Benini S"],"additional_accession":[]},"is_claimable":false,"name":"SidF, a dual substrate N5-acetyl-N5-hydroxy-L-ornithine transacetylase involved in <i>Aspergillus fumigatus</i> siderophore biosynthesis.","description":"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 media","dates":{"release":"2025-01-01T00:00:00Z","publication":"2025 Jun","modification":"2026-06-02T20:50:02.005Z","creation":"2025-04-05T11:34:33.39Z"},"accession":"S-EPMC11751504","cross_references":{"pubmed":["39845173"],"doi":["10.1016/j.yjsbx.2024.100119"]}}