4K3I

Crystal Structure of the Quinol Form of Methylamine Dehydrogenase in Complex with the Diferrous Form of MauG, C2 Space Group

4K3I の概要

• エントリーDOI: 10.2210/pdb4k3i/pdb
• 関連するPDBエントリー: 3SXT
• 分子名称: Methylamine utilization protein MauG, Methylamine dehydrogenase light chain, Methylamine dehydrogenase heavy chain, ... (9 entities in total)
• 機能のキーワード: oxidoreductase
• 由来する生物種: Paracoccus denitrificans; 詳細
• 細胞内の位置: Periplasm: Q51658 P22619
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 199972.19

構造登録者

Yukl, E.Y.,Wilmot, C.M. (登録日: 2013-04-10, 公開日: 2013-07-10, 最終更新日: 2023-12-06)

主引用文献

Yukl, E.T.,Jensen, L.M.,Davidson, V.L.,Wilmot, C.M.
Structures of MauG in complex with quinol and quinone MADH.
Acta Crystallogr.,Sect.F, 69:738-743, 2013

PubMed Abstract: MauG has been cocrystallized with methylamine dehydrogenase (MADH) with its TTQ cofactor in the o-quinol (TTQOQ) and quinone (TTQOX) forms and the structures of the resulting complexes have been solved. The TTQOQ structure crystallized in either space group P21 or C2, while the TTQOX structure crystallized in space group P1. The previously solved structure of MauG in complex with MADH bearing an incompletely formed TTQ cofactor (preMADH) also crystallized in space group P1, although with different unit-cell parameters. Despite the changes in crystal form, the structures are virtually identical, with only very minor changes at the protein-protein interface. The relevance of these structures with respect to the measured changes in affinity between MauG and various forms of MADH is discussed.

PubMed: 23832199
DOI: 10.1107/S1744309113016539

実験手法

X-RAY DIFFRACTION (2 Å)