期刊
ANGEWANDTE CHEMIE-INTERNATIONAL EDITION
卷 57, 期 44, 页码 14624-14629出版社
WILEY-V C H VERLAG GMBH
DOI: 10.1002/anie.201807093
关键词
fungi; hydrolysis; iron metabolism; siderophores; tetrahedral intermediate
资金
- Deutsche Forschungsgemeinschaft [GR 1861/8-1]
- Austrian Science Fund [I1346-B21]
- Young Scholars' Program of the Bavarian Academy of Sciences and Humanities
Fungi utilize high-affinity chelators termed siderophores with chemically diverse structures to scavenge the essential nutrient iron from their surroundings. Since they are among the strongest known Fe3+ binding agents, intracellular release of the heavy metal atom is facilitated by the activity of specific hydrolases. In this work, we report the characterization and X-ray crystal structures of four siderophore esterases: AfEstB and AfSidJ from Aspergillus fumigatus, as well as AnEstB and AnEstA from Aspergillus nidulans. Even though they all display the conserved alpha/beta-hydrolase fold, we found significant structural and enzymatic discrepancies in their adaption to both related and chemically diverse substrates. A structure of AfEstB in complex with its substrate triacetylfusarinine C gives insight into the active enzyme and shows tetrahedral coordination between the catalytic serine and the scissile ester bond.
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