8U42
OvsA from Halomonas utahensis, a selenoxide synthase involved in ovoselenol biosynthesis
Summary for 8U42
| Entry DOI | 10.2210/pdb8u42/pdb |
| Related | 8U41 |
| Descriptor | Selenoxide synthase OvsA, FE (III) ION, SODIUM ION, ... (6 entities in total) |
| Functional Keywords | oxidoreductase, ovoselenol, selenium, selenoxide, nonheme iron |
| Biological source | Halomonas utahensis |
| Total number of polymer chains | 2 |
| Total formula weight | 110003.73 |
| Authors | Ireland, K.A.,Davis, K.M. (deposition date: 2023-09-08, release date: 2024-07-17, Last modification date: 2024-11-13) |
| Primary citation | Kayrouz, C.M.,Ireland, K.A.,Ying, V.Y.,Davis, K.M.,Seyedsayamdost, M.R. Discovery of the selenium-containing antioxidant ovoselenol derived from convergent evolution. Nat.Chem., 16:1868-1875, 2024 Cited by PubMed Abstract: Selenium is an essential micronutrient, but its presence in biology has been limited to protein and nucleic acid biopolymers. The recent identification of a biosynthetic pathway for selenium-containing small molecules suggests that there is a larger family of selenometabolites that remains to be discovered. Here we identify a recently evolved branch of abundant and uncharacterized metalloenzymes that we predict are involved in selenometabolite biosynthesis using a bioinformatic search strategy that relies on the mapping of composite active site motifs. Biochemical studies confirm this prediction and show that these enzymes form an unusual C-Se bond onto histidine, thus giving rise to a distinct selenometabolite and potent antioxidant that we have termed ovoselenol. Aside from providing insights into the evolution of this enzyme class and the structural basis of C-Se bond formation, our work offers a blueprint for charting the microbial selenometabolome in the future. PubMed: 39143299DOI: 10.1038/s41557-024-01600-2 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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