6GUG

Siderophore hydrolase EstB mutant S148A from Aspergillus fumigatus

Summary for 6GUG

• Entry DOI: 10.2210/pdb6gug/pdb
• Descriptor: Siderophore esterase IroE-like, putative, GLYCEROL, SULFATE ION, ... (4 entities in total)
• Functional Keywords: alpha/beta-hydrolase, siderophore, hydrolysis, fungi, hydrolase
• Biological source: Aspergillus fumigatus Af293
• Total number of polymer chains: 2
• Total formula weight: 66062.44

Authors

Ecker, F.,Haas, H.,Groll, M.,Huber, E.M. (deposition date: 2018-06-19, release date: 2018-08-15, Last modification date: 2024-01-17)

Primary citation

Ecker, F.,Haas, H.,Groll, M.,Huber, E.M.
Iron Scavenging in Aspergillus Species: Structural and Biochemical Insights into Fungal Siderophore Esterases.
Angew. Chem. Int. Ed. Engl., 57:14624-14629, 2018

PubMed 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 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 α/β-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.

PubMed: 30070018
DOI: 10.1002/anie.201807093

Experimental method

X-RAY DIFFRACTION (1.45 Å)