Structure Report for: 6GUG

Ecker F, Haas H, Groll M, Huber E

Title: Iron Scavenging in Aspergillus Species: Structural and Biochemical Insights into Fungal Siderophore Esterases
Ecker F, Haas H, Groll M, Huber EM
Ref: Angew Chem Int Ed Engl, 57:14624, 2018 : PubMed
Abstract


ESTHER: Ecker_2018_Angew.Chem.Int.Ed.Engl_57_14624
PubMedSearch: Ecker 2018 Angew.Chem.Int.Ed.Engl 57 14624
PubMedID: 30070018
Gene_locus related to this paper: aspfu-q4wf29, emeni-AnEstB, emeni-q5av79, aspfu-q4wf56

Abstract

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 Fe(3+) 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.