6GUP
Siderophore hydrolase EstB from Aspergillus fumigatus
Summary for 6GUP
| Entry DOI | 10.2210/pdb6gup/pdb |
| Descriptor | Siderophore biosynthesis lipase/esterase, putative, GLYCEROL (3 entities in total) |
| Functional Keywords | alpha/beta-hydrolase, siderophore, hydrolysis, fungi, hydrolase |
| Biological source | Aspergillus fumigatus |
| Total number of polymer chains | 2 |
| Total formula weight | 78127.63 |
| Authors | Ecker, F.,Haas, H.,Groll, M.,Huber, E.M. (deposition date: 2018-06-19, release date: 2018-08-15, Last modification date: 2024-05-15) |
| 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 Cited by 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: 30070018DOI: 10.1002/anie.201807093 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.85 Å) |
Structure validation
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