6Y9C

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

6Y9C の概要

• エントリーDOI: 10.2210/pdb6y9c/pdb
• 関連するPDBエントリー: 6Y8J 6Y8S
• 分子名称: Carnitine monooxygenase oxygenase subunit, FE (III) ION, CARNITINE, ... (6 entities in total)
• 機能のキーワード: apo, rieske, iron-sulphur cluster, oxidoreductase
• 由来する生物種: Acinetobacter baumannii
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 45200.06

構造登録者

Quareshy, M.,Shanmugam, M.,Bugg, T.D.,Cameron, A.,Chen, Y. (登録日: 2020-03-06, 公開日: 2021-03-31, 最終更新日: 2024-01-31)

主引用文献

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

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: 36617384
DOI: 10.1111/febs.16722

実験手法

X-RAY DIFFRACTION (1.8 Å)