1gog
From Proteopedia
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NOVEL THIOETHER BOND REVEALED BY A 1.7 ANGSTROMS CRYSTAL STRUCTURE OF GALACTOSE OXIDASE
Overview
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.
About this Structure
1GOG is a Single protein structure of sequence from Hypomyces rosellus with CU and NA as ligands. Active as Galactose oxidase, with EC number 1.1.3.9 Full crystallographic information is available from OCA.
Reference
Novel thioether bond revealed by a 1.7 A crystal structure of galactose oxidase., Ito N, Phillips SE, Stevens C, Ogel ZB, McPherson MJ, Keen JN, Yadav KD, Knowles PF, Nature. 1991 Mar 7;350(6313):87-90. PMID:2002850
Page seeded by OCA on Tue Nov 20 16:12:15 2007
