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PDBsum entry 1ocr
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Oxidoreductase
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PDB id
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1ocr
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Contents |
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514 a.a.
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227 a.a.
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261 a.a.
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144 a.a.
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109 a.a.
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98 a.a.
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84 a.a.
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79 a.a.
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73 a.a.
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58 a.a.
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49 a.a.
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47 a.a.
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43 a.a.
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 _CU
×6
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 _ZN
×2
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 _MG
×2
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_NA
×2
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* Residue conservation analysis
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References listed in PDB file
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Key reference
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Title
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Redox-Coupled crystal structural changes in bovine heart cytochrome c oxidase.
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Authors
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S.Yoshikawa,
K.Shinzawa-Itoh,
R.Nakashima,
R.Yaono,
E.Yamashita,
N.Inoue,
M.Yao,
M.J.Fei,
C.P.Libeu,
T.Mizushima,
H.Yamaguchi,
T.Tomizaki,
T.Tsukihara.
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Ref.
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Science, 1998,
280,
1723-1729.
[DOI no: ]
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PubMed id
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Abstract
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Crystal structures of bovine heart cytochrome c oxidase in the fully oxidized,
fully reduced, azide-bound, and carbon monoxide-bound states were determined at
2.30, 2.35, 2.9, and 2.8 angstrom resolution, respectively. An aspartate residue
apart from the O2 reduction site exchanges its effective accessibility to the
matrix aqueous phase for one to the cytosolic phase concomitantly with a
significant decrease in the pK of its carboxyl group, on reduction of the metal
sites. The movement indicates the aspartate as the proton pumping site. A
tyrosine acidified by a covalently linked imidazole nitrogen is a possible
proton donor for the O2 reduction by the enzyme.
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Figure 2.
Fig. 2. Crystal structures of the Fe[a3]-Cu[B] site in the
fully reduced CO-bound and fully oxidized azide-bound states and
those of^ the Na^+/Ca^2+ and Mg^2+ sites. (F[o]  F[c])
difference Fourier maps for CO bound at Fe[a3]^ at 3  level (A)
and azide bridging between Fe[a3] and Cu[B]^ at 2.2 level (B)
are given where the bound ligands and^ fixed waters are not
included in the F[c] calculation. The difference^ electron
density maps at 4 level (1
=
0.0436e^-/Å^3) for the Na^+/Ca^2+ site (C) and for the
Mg^2+ site (D). Violet, purple, and blue balls are the
positions^ of Na^+, Mg^2+, and water, respectively.
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Figure 3.
Fig. 3. Redox-coupled conformational change in the segment
from Gly^49 to Asn^55. The conformation of the segment in the
fully oxidized form is^ stereoscopically shown in red, and that
in the fully reduced form^ in green. The yellow structure
denotes subunit II with no redox-coupled^ conformational change.
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The above figures are
reprinted
by permission from the AAAs:
Science
(1998,
280,
1723-1729)
copyright 1998.
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Secondary reference #1
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Title
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The whole structure of the 13-Subunit oxidized cytochrome c oxidase at 2.8 a.
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Authors
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T.Tsukihara,
H.Aoyama,
E.Yamashita,
T.Tomizaki,
H.Yamaguchi,
K.Shinzawa-Itoh,
R.Nakashima,
R.Yaono,
S.Yoshikawa.
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Ref.
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Science, 1996,
272,
1136-1144.
[DOI no: ]
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PubMed id
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Secondary reference #2
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Title
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Structures of metal sites of oxidized bovine heart cytochrome c oxidase at 2.8 a.
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Authors
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T.Tsukihara,
H.Aoyama,
E.Yamashita,
T.Tomizaki,
H.Yamaguchi,
K.Shinzawa-Itoh,
R.Nakashima,
R.Yaono,
S.Yoshikawa.
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Ref.
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Science, 1995,
269,
1069-1074.
[DOI no: ]
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PubMed id
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