1PJ6

Crystal structure of dimethylglycine oxidase of Arthrobacter globiformis in complex with folic acid

1PJ6 の概要

• エントリーDOI: 10.2210/pdb1pj6/pdb
• 関連するPDBエントリー: 1PJ5 1PJ7
• 分子名称: N,N-dimethylglycine oxidase, SODIUM ION, FOLIC ACID, ... (5 entities in total)
• 機能のキーワード: channelling, folate binding, fad binding, amine oxidation, oxidoreductase
• 由来する生物種: Arthrobacter globiformis
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 91325.41

構造登録者

Leys, D.,Basran, J.,Scrutton, N.S. (登録日: 2003-06-01, 公開日: 2003-10-07, 最終更新日: 2024-10-16)

主引用文献

Leys, D.,Basran, J.,Scrutton, N.S.
Channelling and formation of 'active' formaldehyde in dimethylglycine oxidase.
Embo J., 22:4038-4048, 2003

PubMed Abstract: Here we report crystal structures of dimethylglycine oxidase (DMGO) from the bacterium Arthrobacter globiformis, a bifunctional enzyme that catalyzes the oxidation of N,N-dimethyl glycine and the formation of 5,10-methylene tetrahydrofolate. The N-terminal region binds FAD covalently and oxidizes dimethylglycine to a labile iminium intermediate. The C-terminal region binds tetrahydrofolate, comprises three domains arranged in a ring-like structure and is related to the T-protein of the glycine cleavage system. The complex with folinic acid indicates that this enzyme selectively activates the N10 amino group for initial attack on the substrate. Dead-end reactions with oxidized folate are avoided by the strict stereochemical constraints imposed by the folate-binding funnel. The active sites in DMGO are approximately 40 A apart, connected by a large irregular internal cavity. The tetrahydrofolate-binding funnel serves as a transient entry-exit port, and access to the internal cavity is controlled kinetically by tetrahydrofolate binding. The internal cavity enables sequestration of the reactive iminium intermediate prior to reaction with tetrahydrofolate and avoids formation of toxic formaldehyde. This mode of channelling in DMGO is distinct from other channelling mechanisms.

PubMed: 12912903
DOI: 10.1093/emboj/cdg395

実験手法

X-RAY DIFFRACTION (1.65 Å)