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PDBsum entry 1gog
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Oxidoreductase(oxygen(a))
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PDB id
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1gog
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References listed in PDB file
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Key reference
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Title
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Novel thioether bond revealed by a 1.7 a crystal structure of galactose oxidase.
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Authors
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N.Ito,
S.E.Phillips,
C.Stevens,
Z.B.Ogel,
M.J.Mcpherson,
J.N.Keen,
K.D.Yadav,
P.F.Knowles.
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Ref.
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Nature, 1991,
350,
87-90.
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PubMed id
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Abstract
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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.
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Secondary reference #1
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Title
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Crystal structure of a free radical enzyme, Galactose oxidase.
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Authors
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N.Ito,
S.E.Phillips,
K.D.Yadav,
P.F.Knowles.
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Ref.
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J Mol Biol, 1994,
238,
794-814.
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PubMed id
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Note In the PDB file this reference is
annotated as "TO BE PUBLISHED".
The citation details given above were identified by an automated
search of PubMed on title and author
names, giving a
percentage match of
93%.
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Secondary reference #2
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Title
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Galactose oxidase of dactylium dendroides. Gene cloning and sequence analysis.
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Authors
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M.J.Mcpherson,
Z.B.Ogel,
C.Stevens,
K.D.Yadav,
J.N.Keen,
P.F.Knowles.
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Ref.
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J Biol Chem, 1992,
267,
8146-8152.
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PubMed id
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