6LVC

Structure of Dimethylformamidase, dimer

6LVC の概要

• エントリーDOI: 10.2210/pdb6lvc/pdb
• EMDBエントリー: 0988 0989
• 分子名称: N,N-dimethylformamidase large subunit, N,N-dimethylformamidase small subunit, FE (III) ION, ... (4 entities in total)
• 機能のキーワード: ab polypeptide, mononuclear iron, amidohydrolase, tetramer, hydrolase
• 由来する生物種: Paracoccus sp. SSG05; 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 204962.85

構造登録者

Arya, C.A.,Yadav, S.,Fine, J.,Casanal, A.,Chopra, G.,Ramanathan, G.,Subramanian, R.,Vinothkumar, K.R. (登録日: 2020-02-02, 公開日: 2020-06-03, 最終更新日: 2024-03-27)

主引用文献

Arya, C.K.,Yadav, S.,Fine, J.,Casanal, A.,Chopra, G.,Ramanathan, G.,Vinothkumar, K.R.,Subramanian, R.
A 2-Tyr-1-carboxylate Mononuclear Iron Center Forms the Active Site of a Paracoccus Dimethylformamidase.
Angew.Chem.Int.Ed.Engl., 59:16961-16966, 2020

PubMed Abstract: N,N-dimethyl formamide (DMF) is an extensively used organic solvent but is also a potent pollutant. Certain bacterial species from genera such as Paracoccus, Pseudomonas, and Alcaligenes have evolved to use DMF as a sole carbon and nitrogen source for growth via degradation by a dimethylformamidase (DMFase). We show that DMFase from Paracoccus sp. strain DMF is a halophilic and thermostable enzyme comprising a multimeric complex of the α β or (α β ) type. One of the three domains of the large subunit and the small subunit are hitherto undescribed protein folds of unknown evolutionary origin. The active site consists of a mononuclear iron coordinated by two Tyr side-chain phenolates and one carboxylate from Glu. The Fe ion in the active site catalyzes the hydrolytic cleavage of the amide bond in DMF. Kinetic characterization reveals that the enzyme shows cooperativity between subunits, and mutagenesis and structural data provide clues to the catalytic mechanism.

PubMed: 32452120
DOI: 10.1002/anie.202005332

実験手法

ELECTRON MICROSCOPY (3 Å)