1TMX

Crystal structure of hydroxyquinol 1,2-dioxygenase from Nocardioides Simplex 3E

1TMX の概要

• エントリーDOI: 10.2210/pdb1tmx/pdb
• 分子名称: hydroxyquinol 1,2-dioxygenase, FE (III) ION, COPPER (II) ION, ... (8 entities in total)
• 機能のキーワード: beta barrel, oxidoreductase
• 由来する生物種: Pimelobacter simplex
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 66064.12

構造登録者

Ferraroni, M.,Travkin, V.M.,Seifert, J.,Schlomann, M.,Golovleva, L.,Scozzafava, A.,Briganti, F. (登録日: 2004-06-11, 公開日: 2005-03-22, 最終更新日: 2024-02-14)

主引用文献

Ferraroni, M.,Seifert, J.,Travkin, V.M.,Thiel, M.,Kaschabek, S.,Scozzafava, A.,Golovleva, L.,Schlomann, M.,Briganti, F.
Crystal structure of the hydroxyquinol 1,2-dioxygenase from Nocardioides simplex 3E, a key enzyme involved in polychlorinated aromatics biodegradation.
J.Biol.Chem., 280:21144-21154, 2005

PubMed Abstract: Hydroxyquinol 1,2-dioxygenase (1,2-HQD) catalyzes the ring cleavage of hydroxyquinol (1,2,4-trihydroxybenzene), a central intermediate in the degradation of aromatic compounds including a variety of particularly recalcitrant polychloro- and nitroaromatic pollutants. We report here the primary sequence determination and the analysis of the crystal structure of the 1,2-HQD from Nocardioides simplex 3E solved at 1.75 A resolution using the multiple wavelength anomalous dispersion of the two catalytic irons (1 Fe/293 amino acids). The catalytic Fe(III) coordination polyhedron composed by the side chains of Tyr164, Tyr197, His221, and His223 resembles that of the other known intradiol-cleaving dioxygenases, but several of the tertiary structure features are notably different. One of the most distinctive characteristics of the present structure is the extensive openings and consequent exposure to solvent of the upper part of the catalytic cavity arranged to favor the binding of hydroxyquinols but not catechols. A co-crystallized benzoate-like molecule is also found bound to the metal center forming a distinctive hydrogen bond network as observed previously also in 4-chlorocatechol 1,2-dioxygenase from Rhodococcus opacus 1CP. This is the first structure of an intradiol dioxygenase specialized in hydroxyquinol ring cleavage to be investigated in detail.

PubMed: 15772073
DOI: 10.1074/jbc.M500666200

実験手法

X-RAY DIFFRACTION (1.75 Å)