6y9c | pdb_00006y9c

The structure of a quaternary ammonium Rieske monooxygenase reveals insights into carnitine oxidation by gut microbiota and inter-subunit electron transfer

spinqualitylabelsall models 6y9c, resolution 1.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6y9c is a 1 chain structure with sequence from Acinetobacter baumannii. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.8Å Ligands: 152, FE, FES, SCN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function CNTA_ACIB2 Converts carnitine to trimethylamine and malic semialdehyde.[HAMAP-Rule:MF_02097] Publication Abstract from PubMed 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 non-stoichiometric role to ensure the catalytic iron centre remains in an Fe(II) state. Characterisation of an unusual cysteine pair in the Rieske carnitine monooxygenase CntA catalytic site.,Quareshy M, Shanmugam M, Cameron AD, Bugg TDH, Chen Y FEBS J. 2023 Jan 8. doi: 10.1111/febs.16722. PMID:36617384 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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