3ECJ

Structure of E323L mutant of Homoprotocatechuate 2,3-Dioxygenase from Brevibacterium fuscum at 1.65A resolution

3ECJ の概要

• エントリーDOI: 10.2210/pdb3ecj/pdb
• 関連するPDBエントリー: 3ECK
• 分子名称: PROTEIN (Homoprotocatechuate 2,3-dioxygenase), FE (II) ION, CHLORIDE ION, ... (6 entities in total)
• 機能のキーワード: oxidoreductase, oxygenase, extradiol, feii, crystal packing, dioxygenase
• 由来する生物種: Brevibacterium fuscum
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 167915.29

構造登録者

Kovaleva, E.G.,Lipscomb, J.D. (登録日: 2008-08-31, 公開日: 2008-10-07, 最終更新日: 2023-08-30)

主引用文献

Kovaleva, E.G.,Lipscomb, J.D.
Intermediate in the O-O Bond Cleavage Reaction of an Extradiol Dioxygenase.
Biochemistry, 47:11168-11170, 2008

PubMed Abstract: The reactive oxy intermediate of the catalytic cycle of extradiol aromatic ring-cleaving dioxygenases is formed by binding the catecholic substrate and O2 in adjacent ligand positions of the active site metal [usually Fe(II)]. This intermediate and the following Fe(II)-alkylperoxo intermediate resulting from oxygen attack on the substrate have been previously characterized in a crystal of homoprotocatechuate 2,3-dioxygenase (HPCD). Here a subsequent intermediate in which the O-O bond is broken to yield a gem diol species is structurally characterized. This new intermediate is stabilized in the crystal by using the alternative substrate, 4-sulfonylcatechol, and the Glu323Leu variant of HPCD, which alters the crystal packing.

PubMed: 18826259
DOI: 10.1021/bi801459q

実験手法

X-RAY DIFFRACTION (1.65 Å)