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PDBsum entry 1cyc
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Electron transport
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PDB id
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1cyc
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Contents |
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* Residue conservation analysis
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J Biochem (tokyo)
77:147-162
(1975)
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PubMed id:
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The crystal structure of bonito (katsuo) ferrocytochrome c at 2.3 A resolution. II. Structure and function.
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N.Tanaka,
T.Yamane,
T.Tsukihara,
T.Ashida,
M.Kakudo.
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ABSTRACT
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The structure analysis of bonito heart ferrocytochrome c was carried out at 2.3
A resolution by X-ray diffraction, and a Kendrew-type skeletal model was built
up. This molecule has an overall egg shape, 35 A in height, 30 A in width and 23
A in thickness; the 5th ligand of the heme iron atom is the N-epsilon atom of
the His-18 imidazole ring and the 6th is the Met-80 sulfur atom. Distinct
alpha-helix regions are found between the N-terminus and reside 11, between 60
and 69, and between 90 and the C-terminus. The most distinct difference between
the conformation of the present molecule and that of the horse oxidized molecule
is the location of the Phe-82 phenyl ring. In the present reduced molecule, the
phyenyl ring is in closer contact with the iron atom and gives influences on the
character of the iron atom. Inside the molecule, at the lower part of the heme
pocket, there is an extended hydrogen bond network including the propionic acid
residues of the heme group. Both Phe-82 and the hydrogen bond network may play a
key role in the function of this molecule.
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Literature references that cite this PDB file's key reference
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PubMed id
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Reference
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L.Giachini,
F.Francia,
L.Cordone,
F.Boscherini,
and
G.Venturoli
(2007).
Cytochrome C in a dry trehalose matrix: structural and dynamical effects probed by x-ray absorption spectroscopy.
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Biophys J,
92,
1350-1360.
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S.Yamada,
S.Y.Park,
H.Shimizu,
Y.Koshizuka,
K.Kadokura,
T.Satoh,
K.Suruga,
M.Ogawa,
Y.Isogai,
T.Nishio,
Y.Shiro,
and
T.Oku
(2000).
Structure of cytochrome c6 from the red alga Porphyra yezoensis at 1. 57 A resolution.
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Acta Crystallogr D Biol Crystallogr,
56,
1577-1582.
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PDB code:
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J.S.Fetrow,
U.Dreher,
D.J.Wiland,
D.L.Schaak,
and
T.L.Boose
(1998).
Mutagenesis of histidine 26 demonstrates the importance of loop-loop and loop-protein interactions for the function of iso-1-cytochrome c.
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Protein Sci,
7,
994.
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M.Romanowski,
and
P.S.Song
(1992).
Structural domains of phytochrome deduced from homologies in amino acid sequences.
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J Protein Chem,
11,
139-155.
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J.M.Pachence,
S.Amador,
G.Maniara,
J.Vanderkooi,
P.L.Dutton,
and
J.K.Blasie
(1990).
Orientation and lateral mobility of cytochrome c on the surface of ultrathin lipid multilayer films.
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Biophys J,
58,
379-389.
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T.Takano,
and
R.E.Dickerson
(1980).
Redox conformation changes in refined tuna cytochrome c.
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Proc Natl Acad Sci U S A,
77,
6371-6375.
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PDB codes:
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A.M.Solinger,
M.E.Ultee,
E.Margoliash,
and
R.H.Schwartz
(1979).
T-lymphocyte response to cytochrome c. I. Demonstration of a T-cell heteroclitic proliferative response and identification of a topographic antigenic determinant on pigeon cytochrome c whose immune recognition requires two complementing major histocompatibility complex-linked immune response genes.
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J Exp Med,
150,
830-848.
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The most recent references are shown first.
Citation data come partly from CiteXplore and partly
from an automated harvesting procedure. Note that this is likely to be
only a partial list as not all journals are covered by
either method. However, we are continually building up the citation data
so more and more references will be included with time.
Where a reference describes a PDB structure, the PDB
code is
shown on the right.
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Links
