9ZSC
Flavophos biosynthetic enzyme BsfD
Summary for 9ZSC
| Entry DOI | 10.2210/pdb9zsc/pdb |
| Descriptor | 3-keto-5-aminohexanoate cleavage protein, ZINC ION, SULFATE ION, ... (4 entities in total) |
| Functional Keywords | phosphonate bkace, biosynthetic protein |
| Biological source | Burkholderia stagnalis |
| Total number of polymer chains | 1 |
| Total formula weight | 32488.60 |
| Authors | Ongpipatannakul, C.,Nair, S.K. (deposition date: 2025-12-22, release date: 2026-05-13, Last modification date: 2026-05-20) |
| Primary citation | Simon, M.A.,Ramos-Figueroa, J.S.,Reyes Lopez, V.,Ongpipattanakul, C.,Zhu, L.,Giurgiu, C.,Hoffpauir, Z.A.,Lamb, A.L.,Nair, S.K.,van der Donk, W.A. Discovery of the Phosphonate Flavophos Produced by Burkholderia . J.Am.Chem.Soc., 148:18030-18043, 2026 Cited by PubMed Abstract: Phosphonate natural products have proven value to society as antibiotics and herbicides. They inhibit a range of enzyme targets usually by mimicking the enzyme substrates. In this study, we investigate a family of phosphonate biosynthetic gene clusters (BGCs) found in . Heterologous expression in resulted in production of an antimicrobial compound. Spectroscopic characterization and chemical synthesis assigned its structure as 2,4-dioxopentylphosphonic acid. One of the biosynthetic enzymes is a member of the domain of unknown function (DUF) 849 family with homology to β-keto acid cleavage enzymes (BKACEs). In vitro characterization shows that this enzyme catalyzes chemistry that is divergent from previously characterized BKACEs. The observed catalytic activity is explained by a series of cocrystal structures with substrates and intermediates. The BGC also contains a gene encoding lumazine synthase (LS), an essential enzyme in flavin biosynthesis. Biochemical experiments revealed that 2,4-dioxopentylphosphonic acid inhibits LS. In addition, expression of the LS encoded in the BGC, or LS orthologs from a range of organisms, in conferred resistance to the new phosphonate, which we therefore name flavophos. PubMed: 42036871DOI: 10.1021/jacs.6c01748 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.72 Å) |
Structure validation
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