6TEE
Crystal structure of monooxygenase RutA under anaerobic conditions.
This is a non-PDB format compatible entry.
Summary for 6TEE
| Entry DOI | 10.2210/pdb6tee/pdb |
| Related | 6SGG |
| Descriptor | Pyrimidine monooxygenase RutA, GLYCEROL, FLAVIN MONONUCLEOTIDE, ... (4 entities in total) |
| Functional Keywords | monooxygenase, ruta, fmn, flavin-n5-oxide, bioengineering, flavoprotein |
| Biological source | Escherichia coli K-12 |
| Total number of polymer chains | 1 |
| Total formula weight | 40528.57 |
| Authors | Saleem-Batcha, R.,Matthews, A.,Teufel, R. (deposition date: 2019-11-11, release date: 2020-02-05, Last modification date: 2024-01-24) |
| Primary citation | Matthews, A.,Saleem-Batcha, R.,Sanders, J.N.,Stull, F.,Houk, K.N.,Teufel, R. Aminoperoxide adducts expand the catalytic repertoire of flavin monooxygenases. Nat.Chem.Biol., 16:556-563, 2020 Cited by PubMed Abstract: One of the hallmark reactions catalyzed by flavin-dependent enzymes is the incorporation of an oxygen atom derived from dioxygen into organic substrates. For many decades, these flavin monooxygenases were assumed to use exclusively the flavin-C4a-(hydro)peroxide as their oxygen-transferring intermediate. We demonstrate that flavoenzymes may instead employ a flavin-N5-peroxide as a soft α-nucleophile for catalysis, which enables chemistry not accessible to canonical monooxygenases. This includes, for example, the redox-neutral cleavage of carbon-hetero bonds or the dehalogenation of inert environmental pollutants via atypical oxygenations. We furthermore identify a shared structural motif for dioxygen activation and N5-functionalization, suggesting a conserved pathway that may be operative in numerous characterized and uncharacterized flavoenzymes from diverse organisms. Our findings show that overlooked flavin-N5-oxygen adducts are more widespread and may facilitate versatile chemistry, thus upending the notion that flavin monooxygenases exclusively function as nature's equivalents to organic peroxides in synthetic chemistry. PubMed: 32066967DOI: 10.1038/s41589-020-0476-2 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.2 Å) |
Structure validation
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