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PDBsum entry 2zwf
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Oxidoreductase/metal transport
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PDB id
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2zwf
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References listed in PDB file
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Key reference
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Title
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Crystallographic evidence of drastic movement of a copper ion toward the substrate tyrosine for starting hydroxylation reaction of tyrosinase
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Authors
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Y.Matoba,
H.Yoshitsu,
H.J.Jeon,
K.Oda,
M.Noda,
T.Kumagai,
M.Sugiyama.
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Ref.
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TO BE PUBLISHED ...
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Secondary reference #1
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Title
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Crystallographic evidence that the dinuclear copper center of tyrosinase is flexible during catalysis.
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Authors
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Y.Matoba,
T.Kumagai,
A.Yamamoto,
H.Yoshitsu,
M.Sugiyama.
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Ref.
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J Biol Chem, 2006,
281,
8981-8990.
[DOI no: ]
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PubMed id
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Figure 5.
FIGURE 5. Structural similarity. A, stereo representation
of the superposition of tyrosinase and structurally homologous
proteins, potato catechol oxidase (Protein Data Bank code 1BT1)
and octopus hemocyanin (Protein Data Bank code 1JS8). Red, blue,
and green indicate the backbone traces of tyrosinase, catechol
oxidase, and hemocyanin, respectively. The yellow sphere
indicates the two copper ions in the catalytic center. To
emphasize similarity, the C-terminal domain of hemocyanin is
omitted from the figure. B, stereo view of the superposition of
ORF378 and the SH2 domain in the growth factor-bound protein 2
(Protein Data Bank code 1GRI). Red and blue indicate the
backbone trace of ORF378 and the SH2 domain in the growth
factor-bound protein 2, respectively.
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Figure 9.
FIGURE 9. Structure-based catalytic mechanism of
tyrosinase. The oxy form of tyrosinase catalyzes the conversion
of monophenol to the corresponding quinone through the
ortho-diphenol formation. In this scheme, His^54 is released
from the Cu^A site, resulting in the formation of the bidentate
intermediate. The met and oxy forms of tyrosinase can catalyze
the conversion of ortho-diphenol to the corresponding quinone.
This reaction should progress similarly to that of catechol
oxidase.
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The above figures are
reproduced from the cited reference
with permission from the ASBMB
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