2CKF

Crystal Structure of the Terminal Component of the PAH-hydroxylating Dioxygenase from Sphingomonas sp CHY-1

2CKF の概要

• エントリーDOI: 10.2210/pdb2ckf/pdb
• 分子名称: RING-HYDROXYLATING DIOXYGENASE ALPHA SUBUNIT, RING-HYDROXYLATING DIOXYGENASE BETA SUBUNIT, FE2/S2 (INORGANIC) CLUSTER, ... (5 entities in total)
• 機能のキーワード: rieske non heme iron dioxygenase, pyrene dioxygenase, ring-hydroxylating dioxygenase, high-molecular-weight polycyclic aromatic hydrocarbons, oxidoreductase
• 由来する生物種: SPHINGOMONAS SP.; 詳細
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 215737.76

構造登録者

Jakoncic, J.,Meyer, C.,Jouanneau, Y.,Stojanoff, V. (登録日: 2006-04-18, 公開日: 2007-01-02, 最終更新日: 2024-05-01)

主引用文献

Jakoncic, J.,Jouanneau, Y.,Meyer, C.,Stojanoff, V.
The Catalytic Pocket of the Ring-Hydroxylating Dioxygenase from Sphingomonas Chy-1.
Biochem.Biophys.Res.Commun., 352:861-, 2007

PubMed Abstract: Ring-hydroxylating dioxygenases are multicomponent bacterial enzymes that catalyze the first step in the oxidative degradation of aromatic hydrocarbons. The dioxygenase from Sphingomonas CHY-1 is unique in that it can oxidize a wide range of polycyclic aromatic hydrocarbons (PAHs). With a crystal structure similar to that of the seven other known dioxygenases, its catalytic domain features the largest hydrophobic substrate binding cavity characterized so far. Molecular modeling studies indicated that the catalytic cavity is large enough to accommodate a five-ring benzo[a]pyrene molecule. The predicted positions of this and other PAHs in the substrate binding pocket are consistent with the product regio- and stereo-selectivity of the enzyme.

PubMed: 17157819
DOI: 10.1016/J.BBRC.2006.11.117

実験手法

X-RAY DIFFRACTION (1.85 Å)