1goh: Difference between revisions

Revision as of 13:52, 21 February 2008

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

OverviewOverview

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 StructureAbout this Structure

1GOH is a Single protein structure of sequence from Hypomyces rosellus with as ligand. Active as Galactose oxidase, with EC number 1.1.3.9 Full crystallographic information is available from OCA.

ReferenceReference

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 Thu Feb 21 12:52:19 2008

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OCA

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-[[Image:1goh.gif|left|200px]]<br /><applet load="1goh" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1goh.gif|left|200px]]<br /><applet load="1goh" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1goh, resolution 2.2&Aring;" />
 '''NOVEL THIOETHER BOND REVEALED BY A 1.7 ANGSTROMS CRYSTAL STRUCTURE OF GALACTOSE OXIDASE'''<br />
 ==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.
+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==
-GOH is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Hypomyces_rosellus Hypomyces rosellus] with NA as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Galactose_oxidase Galactose oxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.3.9 1.1.3.9] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1GOH OCA].
+GOH is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Hypomyces_rosellus Hypomyces rosellus] with <scene name='pdbligand=NA:'>NA</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Galactose_oxidase Galactose oxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.3.9 1.1.3.9] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GOH OCA].
 ==Reference==
@@ Line 15: / Line 15: @@
 [[Category: Single protein]]
 [[Category: Ito, N.]]
-[[Category: Knowles, P.F.]]
+[[Category: Knowles, P F.]]
-[[Category: Phillips, S.E.V.]]
+[[Category: Phillips, S E.V.]]
 [[Category: NA]]
 [[Category: oxidoreductase(oxygen(a))]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 16:12:19 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:52:19 2008''