1gog

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[[Image:1gog.gif|left|200px]]
[[Image:1gog.gif|left|200px]]
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{{Structure
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|PDB= 1gog |SIZE=350|CAPTION= <scene name='initialview01'>1gog</scene>, resolution 1.9&Aring;
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The line below this paragraph, containing "STRUCTURE_1gog", creates the "Structure Box" on the page.
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|SITE=
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|LIGAND= <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <span class='plainlinks'>[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] </span>
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|GENE=
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{{STRUCTURE_1gog| PDB=1gog | SCENE= }}
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1gog FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gog OCA], [http://www.ebi.ac.uk/pdbsum/1gog PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1gog RCSB]</span>
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'''NOVEL THIOETHER BOND REVEALED BY A 1.7 ANGSTROMS CRYSTAL STRUCTURE OF GALACTOSE OXIDASE'''
'''NOVEL THIOETHER BOND REVEALED BY A 1.7 ANGSTROMS CRYSTAL STRUCTURE OF GALACTOSE OXIDASE'''
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[[Category: Knowles, P F.]]
[[Category: Knowles, P F.]]
[[Category: Phillips, S E.V.]]
[[Category: Phillips, S E.V.]]
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[[Category: oxidoreductase(oxygen(a))]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 17:49:19 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:48:13 2008''
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Revision as of 14:49, 2 May 2008

Image:1gog.gif

Template:STRUCTURE 1gog

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. 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 Fri May 2 17:49:19 2008

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