1goh: Difference between revisions
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|PDB= 1goh |SIZE=350|CAPTION= <scene name='initialview01'>1goh</scene>, resolution 2.2Å | |PDB= 1goh |SIZE=350|CAPTION= <scene name='initialview01'>1goh</scene>, resolution 2.2Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand=NA:SODIUM ION'>NA</scene> | |LIGAND= <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=1goh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1goh OCA], [http://www.ebi.ac.uk/pdbsum/1goh PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1goh 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: 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 20:48:10 2008'' | ||
Revision as of 20:48, 30 March 2008
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| , resolution 2.2Å | |||||||
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| 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
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. 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
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