6Y9C
The structure of a quaternary ammonium Rieske monooxygenase reveals insights into carnitine oxidation by gut microbiota and inter-subunit electron transfer
Summary for 6Y9C
| Entry DOI | 10.2210/pdb6y9c/pdb |
| Related | 6Y8J 6Y8S |
| Descriptor | Carnitine monooxygenase oxygenase subunit, FE (III) ION, CARNITINE, ... (6 entities in total) |
| Functional Keywords | apo, rieske, iron-sulphur cluster, oxidoreductase |
| Biological source | Acinetobacter baumannii |
| Total number of polymer chains | 1 |
| Total formula weight | 45200.06 |
| Authors | Quareshy, M.,Shanmugam, M.,Bugg, T.D.,Cameron, A.,Chen, Y. (deposition date: 2020-03-06, release date: 2021-03-31, Last modification date: 2024-01-31) |
| Primary citation | Quareshy, M.,Shanmugam, M.,Cameron, A.D.,Bugg, T.D.H.,Chen, Y. Characterisation of an unusual cysteine pair in the Rieske carnitine monooxygenase CntA catalytic site. Febs J., 2023 Cited by PubMed Abstract: Rieske monooxygenases undertake complex catalysis integral to marine, terrestrial and human gut-ecosystems. Group-I to -IV Rieske monooxygenases accept aromatic substrates and have well-characterised catalytic mechanisms. Nascent to our understanding are Group-V members catalysing the oxidation/breakdown of quaternary ammonium substrates. Phylogenetic analysis of Group V highlights a cysteine residue-pair adjacent to the mononuclear Fe active site with no established role. Following our elucidation of the carnitine monooxygenase CntA structure, we probed the function of the cysteine pair Cys206/Cys209. Utilising biochemical and biophysical techniques, we found the cysteine residues do not play a structural role nor influence the electron transfer pathway, but rather are used in a nonstoichiometric role to ensure the catalytic iron centre remains in an Fe(II) state. PubMed: 36617384DOI: 10.1111/febs.16722 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.8 Å) |
Structure validation
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