8UC3
Cryo-EM structure of the AlbAB cyclodipeptide oxidase enzyme filament
Summary for 8UC3
| Entry DOI | 10.2210/pdb8uc3/pdb |
| EMDB information | 42114 |
| Descriptor | Albonoursin synthase, Protein AlbB, FLAVIN MONONUCLEOTIDE (3 entities in total) |
| Functional Keywords | cyclodipeptide oxidase, cyclic dipeptide oxidase, nitroreductase-like, enzyme filament, flavoenzyme, oxidoreductase |
| Biological source | Streptomyces noursei ATCC 11455 More |
| Total number of polymer chains | 4 |
| Total formula weight | 66221.59 |
| Authors | Andreas, M.P.,Giessen, T.W. (deposition date: 2023-09-25, release date: 2024-05-15, Last modification date: 2024-10-16) |
| Primary citation | Andreas, M.P.,Giessen, T.W. Cyclodipeptide oxidase is an enzyme filament. Nat Commun, 15:3574-3574, 2024 Cited by PubMed Abstract: Modified cyclic dipeptides represent a widespread class of secondary metabolites with diverse pharmacological activities, including antibacterial, antifungal, and antitumor. Here, we report the structural characterization of the Streptomyces noursei enzyme AlbAB, a cyclodipeptide oxidase (CDO) carrying out α,β-dehydrogenations during the biosynthesis of the antibiotic albonoursin. We show that AlbAB is a megadalton heterooligomeric enzyme filament containing covalently bound flavin mononucleotide cofactors. We highlight that AlbAB filaments consist of alternating dimers of AlbA and AlbB and that enzyme activity is crucially dependent on filament formation. We show that AlbA-AlbB interactions are highly conserved suggesting that other CDO-like enzymes are likely enzyme filaments. As CDOs have been employed in the structural diversification of cyclic dipeptides, our results will be useful for future applications of CDOs in biocatalysis and chemoenzymatic synthesis. PubMed: 38678027DOI: 10.1038/s41467-024-48030-9 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (2.78 Å) |
Structure validation
Download full validation report
