1gog
From Proteopedia
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|PDB= 1gog |SIZE=350|CAPTION= <scene name='initialview01'>1gog</scene>, resolution 1.9Å | |PDB= 1gog |SIZE=350|CAPTION= <scene name='initialview01'>1gog</scene>, resolution 1.9Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene> | + | |LIGAND= <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene> |
| - | |ACTIVITY= [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] | + | |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> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |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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[[Category: Knowles, P F.]] | [[Category: Knowles, P F.]] | ||
[[Category: Phillips, S E.V.]] | [[Category: Phillips, S E.V.]] | ||
| - | [[Category: CU]] | ||
| - | [[Category: NA]] | ||
[[Category: oxidoreductase(oxygen(a))]] | [[Category: oxidoreductase(oxygen(a))]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:48:13 2008'' |
Revision as of 17:48, 30 March 2008
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| , resolution 1.9Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Activity: | Galactose oxidase, with EC number 1.1.3.9 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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
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