8CM5

W-formate dehydrogenase C872A from Desulfovibrio vulgaris

8CM5 の概要

• エントリーDOI: 10.2210/pdb8cm5/pdb
• 分子名称: Formate dehydrogenase, alpha subunit, selenocysteine-containing, Formate dehydrogenase, beta subunit, putative, DI(HYDROXYETHYL)ETHER, ... (9 entities in total)
• 機能のキーワード: formate, co2, molybdenum and tungsten enzymes, dmso reductase family, electron transport, oxidoreductase
• 由来する生物種: Desulfovibrio vulgaris str. Hildenborough; 詳細
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 558729.07

構造登録者

Vilela-Alves, G.,Mota, C.,Klymanska, K.,Oliveira, A.R.,Manuel, R.R.,Pereira, I.C.,Romao, M.J. (登録日: 2023-02-17, 公開日: 2023-09-27, 最終更新日: 2024-01-03)

主引用文献

Oliveira, A.R.,Mota, C.,Vilela-Alves, G.,Manuel, R.R.,Pedrosa, N.,Fourmond, V.,Klymanska, K.,Leger, C.,Guigliarelli, B.,Romao, M.J.,Cardoso Pereira, I.A.
An allosteric redox switch involved in oxygen protection in a CO 2 reductase.
Nat.Chem.Biol., 20:111-119, 2024

PubMed Abstract: Metal-dependent formate dehydrogenases reduce CO with high efficiency and selectivity, but are usually very oxygen sensitive. An exception is Desulfovibrio vulgaris W/Sec-FdhAB, which can be handled aerobically, but the basis for this oxygen tolerance was unknown. Here we show that FdhAB activity is controlled by a redox switch based on an allosteric disulfide bond. When this bond is closed, the enzyme is in an oxygen-tolerant resting state presenting almost no catalytic activity and very low formate affinity. Opening this bond triggers large conformational changes that propagate to the active site, resulting in high activity and high formate affinity, but also higher oxygen sensitivity. We present the structure of activated FdhAB and show that activity loss is associated with partial loss of the metal sulfido ligand. The redox switch mechanism is reversible in vivo and prevents enzyme reduction by physiological formate levels, conferring a fitness advantage during O exposure.

PubMed: 37985883
DOI: 10.1038/s41589-023-01484-2

実験手法

X-RAY DIFFRACTION (2.15 Å)