1GOF

NOVEL THIOETHER BOND REVEALED BY A 1.7 ANGSTROMS CRYSTAL STRUCTURE OF GALACTOSE OXIDASE

1GOF の概要

• エントリーDOI: 10.2210/pdb1gof/pdb
• 分子名称: GALACTOSE OXIDASE, COPPER (II) ION, SODIUM ION, ... (5 entities in total)
• 機能のキーワード: oxidoreductase(oxygen(a))
• 由来する生物種: Hypomyces rosellus
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 68785.23

構造登録者

Ito, N.,Phillips, S.E.V.,Knowles, P.F. (登録日: 1993-09-30, 公開日: 1994-01-31, 最終更新日: 2024-10-30)

主引用文献

Ito, N.,Phillips, S.E.,Stevens, C.,Ogel, Z.B.,McPherson, M.J.,Keen, J.N.,Yadav, K.D.,Knowles, P.F.
Novel thioether bond revealed by a 1.7 A crystal structure of galactose oxidase.
Nature, 350:87-90, 1991

PubMed Abstract: Galactose oxidase is an extracellular enzyme secreted by the fungus Dactylium dendroides. It is monomeric, with a relative molecular mass of 68,000, catalyses the stereospecific oxidation of a broad range of primary alcohol substrates and possesses a unique mononuclear copper site essential for catalysing a two-electron transfer reaction during the oxidation of primary alcohols to corresponding aldehydes. Recent evidence arguing against a Cu(III)-Cu(I) couple implies the existence of a second redox-active site proposed to involve pyrroloquinoline quinone or a tyrosine radical. We now report the crystal structure of galactose oxidase at 1.7 A resolution. This reveals a unique structural feature at the copper site with a novel thioether bond linking Cys 228 and Tyr 272 in a stacking interaction with Trp 290. We propose that these molecular components stabilize the protein free-radical species essential for catalysis and thus provide a 'built-in' secondary cofactor. This feature may represent a new mechanism for mediating electron transfer in metalloenzymes in the absence of exogenous cofactors.

PubMed: 2002850
DOI: 10.1038/350087a0

実験手法

X-RAY DIFFRACTION (1.7 Å)