9YPI
MboA HDO apo structure
Summary for 9YPI
| Entry DOI | 10.2210/pdb9ypi/pdb |
| Descriptor | Mangotoxin biosynthesis protein MboA, CHLORIDE ION, SULFATE ION, ... (6 entities in total) |
| Functional Keywords | heme-oxygenase like domain containing enzyme, hdo, di-iron oxidase, alkynase, biosynthetic protein |
| Biological source | Pseudomonas syringae |
| Total number of polymer chains | 4 |
| Total formula weight | 115064.60 |
| Authors | Badding, E.D.,Kissman, E.N.,Chang, M.C.Y. (deposition date: 2025-10-14, release date: 2026-05-06, Last modification date: 2026-05-20) |
| Primary citation | Badding, E.D.,Kissman, E.N.,Velculescu, S.V.,Chang, M.C.Y. Discovery of a Structurally Distinct Acetylenase in the Biosynthesis of Mangotoxin. J.Am.Chem.Soc., 148:18724-18732, 2026 Cited by PubMed Abstract: Amino acids, peptides, and proteins play pivotal roles in medicine, materials, and catalysis, with their functions largely dictated by their side-chain functionality. Recent studies have shown that heme oxygenase-like domain-containing oxidases (HDOs) catalyze a broad range of interesting chemical reactions on amino acids and their derivatives to produce structurally diverse target structures. Using a bioinformatics approach, the mangotoxin biosynthetic operon was found to house an unannotated HDO, MboA, along with a dedicated redox partner, MboB. We show that MboA catalyzes alkyne formation by iterative desaturations on the side-chain of a peptide substrate, where the transformation between alkene and alkyne is gated by MboB. The crystal structure of Fe(II)-MboA reveals an unexpectedly short Fe-Fe distance, suggesting that the activation of strong C(sp)-H bonds may utilize a mechanism distinct from other HDOs and expands the scope of known HDO chemistry. PubMed: 42048656DOI: 10.1021/jacs.5c21680 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.49 Å) |
Structure validation
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