8UX5

OvsA M401Y/Q430N/A431F from Halomonas utahensis, a hercynine-binding variant with selenoneine-biosynthetic activity

Summary for 8UX5

• Entry DOI: 10.2210/pdb8ux5/pdb
• Related: 8U41 8U42
• Descriptor: Selenoxide synthase OvsA, FE (III) ION, SODIUM ION, ... (4 entities in total)
• Functional Keywords: hercynine, selenoneine, selenium, selenoxide, oxidoreductase
• Biological source: Halomonas utahensis
• Total number of polymer chains: 2
• Total formula weight: 110131.90

Authors

Ireland, K.A.,Davis, K.M. (deposition date: 2023-11-08, 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

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: 39143299
DOI: 10.1038/s41557-024-01600-2

Experimental method

X-RAY DIFFRACTION (3.06 Å)