3DHG

Crystal Structure of Toluene 4-Monoxygenase Hydroxylase

3DHG の概要

• エントリーDOI: 10.2210/pdb3dhg/pdb
• 分子名称: toluene 4-monooxygenase hydroxylase alpha subunit, toluene 4-monooxygenase hydroxylase beta subunit, toluene 4-monooxygenase hydroxylase gamma subunit, ... (7 entities in total)
• 機能のキーワード: multicomponent monooxygenase, aromatic hydrocarbons catabolism, fad, flavoprotein, iron, monooxygenase, oxidoreductase
• 由来する生物種: Pseudomonas mendocina; 詳細
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 212951.23

構造登録者

Bailey, L.J.,Mccoy, J.G.,Phillips Jr., G.N.,Fox, B.G. (登録日: 2008-06-17, 公開日: 2008-12-30, 最終更新日: 2024-02-21)

主引用文献

Bailey, L.J.,McCoy, J.G.,Phillips Jr., G.N.,Fox, B.G.
Structural consequences of effector protein complex formation in a diiron hydroxylase.
Proc.Natl.Acad.Sci.USA, 105:19194-19198, 2008

PubMed Abstract: Carboxylate-bridged diiron hydroxylases are multicomponent enzyme complexes responsible for the catabolism of a wide range of hydrocarbons and as such have drawn attention for their mechanism of action and potential uses in bioremediation and enzymatic synthesis. These enzyme complexes use a small molecular weight effector protein to modulate the function of the hydroxylase. However, the origin of these functional changes is poorly understood. Here, we report the structures of the biologically relevant effector protein-hydroxylase complex of toluene 4-monooxygenase in 2 redox states. The structures reveal a number of coordinated changes that occur up to 25 A from the active site and poise the diiron center for catalysis. The results provide a structural basis for the changes observed in a number of the measurable properties associated with effector protein binding. This description provides insight into the functional role of effector protein binding in all carboxylate-bridged diiron hydroxylases.

PubMed: 19033467
DOI: 10.1073/pnas.0807948105

実験手法

X-RAY DIFFRACTION (1.85 Å)