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PDBsum entry 1rie
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Electron transport
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PDB id
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1rie
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References listed in PDB file
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Key reference
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Title
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Structure of a water soluble fragment of the 'Rieske' Iron-Sulfur protein of the bovine heart mitochondrial cytochrome bc1 complex determined by mad phasing at 1.5 a resolution.
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Authors
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S.Iwata,
M.Saynovits,
T.A.Link,
H.Michel.
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Ref.
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Structure, 1996,
4,
567-579.
[DOI no: ]
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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
88%.
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Abstract
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BACKGROUND: The 'Rieske' iron-sulfur protein is the primary electron acceptor
during hydroquinone oxidation in cytochrome bc complexes. The spectroscopic and
electrochemical properties of the 'Rieske' [2Fe-2S] cluster differ significantly
from those of other iron-sulfur clusters. A 129-residue water soluble fragment
containing the intact [2Fe-2S] cluster was isolated following proteolytic
digestion of the bc1 complex and used for structural studies. RESULTS: The
structure of the Rieske iron-sulfur fragment containing the reduced [2Fe-2S]
cluster has been determined using the multiwavelength anomalous diffraction
(MAD) technique and refined at 1.5 A resolution. The fragment has a novel
overall fold that includes three sheets of beta strands. The iron atoms of the
[2Fe-2S] cluster are coordinated by two cysteine (Fe-1) and two histidine (Fe-2)
residues, respectively, with the histidine ligands completely exposed to the
solvent. This is in contrast to the four cysteine coordination pattern observed
in previously characterised [2Fe-2S] ferredoxins. The cluster-binding fold is
formed by two loops connected by a disulfide bridge; these loops superpose with
the metal-binding loops of rubredoxins. The environment of the cluster is
stabilised by an extensive hydrogen-bond network. CONCLUSIONS: The
high-resolution structure supports the proposed coordination pattern involving
histidine ligands and provides a basis for a detailed analysis of the
spectroscopic and electrochemical properties. As the cluster is located at the
tip of the protein, it might come into close contact with cytochrome b. The
exposed N epsilon atoms of the histidine ligands of the cluster are readily
accessible to quinones and inhibitors within the hydroquinone oxidation (QP)
pocket of the bc1 complex and may undergo redox-dependent
protonation/deprotonation.
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Figure 3.
Figure 3. Topology of the ISF. The hydrogen-bond pattern and
secondary structure assignment are indicated. The residues
conserved in all known Rieske iron–sulfur proteins from
cytochrome bc[1] complexes are printed in red. The outlined
characters denote residues missing in Rieske iron–sulfur
protein from the cytochrome b[6]^f complex. Metal ligands and
residues that form a disulfide bridge are colored yellow and
green, respectively. Figure 3. Topology of the ISF. The
hydrogen-bond pattern and secondary structure assignment are
indicated. The residues conserved in all known Rieske
iron–sulfur proteins from cytochrome bc[1] complexes are
printed in red. The outlined characters denote residues missing
in Rieske iron–sulfur protein from the cytochrome b[6]^f
complex. Metal ligands and residues that form a disulfide bridge
are colored yellow and green, respectively.
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Figure 6.
Figure 6. Electrostatic surface properties of the ISF.
Molecular surface of ISF color-coded by electrostatic potential:
red, negative; blue, positive. The extreme ranges of red and
blue represent electrostatic potentials of −5 and +5 k[B]T,
respectively (k[B], Boltzmann constant; T, temperature). The
view shows the same orientation as Figure 2a. The figure was
generated using the program GRASP [50]. Figure 6.
Electrostatic surface properties of the ISF. Molecular
surface of ISF color-coded by electrostatic potential: red,
negative; blue, positive. The extreme ranges of red and blue
represent electrostatic potentials of −5 and +5 k[B]T,
respectively (k[B], Boltzmann constant; T, temperature). The
view shows the same orientation as [3]Figure 2a. The figure was
generated using the program GRASP [4][50].
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The above figures are
reprinted
by permission from Cell Press:
Structure
(1996,
4,
567-579)
copyright 1996.
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Secondary reference #1
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Title
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Isolation, Characterisation and crystallisation of a water-Soluble fragment of the rieske iron-Sulfur protein of bovine heart mitochondrial bc1 complex.
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Authors
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T.A.Link,
M.Saynovits,
C.Assmann,
S.Iwata,
T.Ohnishi,
G.Von jagow.
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Ref.
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Eur J Biochem, 1996,
237,
71-75.
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PubMed id
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Secondary reference #2
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Title
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The mitochondrial targeting presequence of the rieske iron-Sulfur protein is processed in a single step after insertion into the cytochrome bc1 complex in mammals and retained as a subunit in the complex.
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Authors
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U.Brandt,
L.Yu,
C.A.Yu,
B.L.Trumpower.
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Ref.
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J Biol Chem, 1993,
268,
8387-8390.
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PubMed id
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Secondary reference #3
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Title
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Cloning and sequencing of a cdna encoding the rieske iron-Sulfur protein of bovine heart mitochondrial ubiquinol-Cytochrome c reductase.
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Authors
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S.Usui,
L.Yu,
C.A.Yu.
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Ref.
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Biochem Biophys Res Commun, 1990,
167,
575-579.
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PubMed id
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Secondary reference #4
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Title
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Isolation and amino acid sequence of the 'Rieske' Iron sulfur protein of beef heart ubiquinol:cytochrome c reductase.
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Authors
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H.Schägger,
U.Borchart,
W.Machleidt,
T.A.Link,
G.Von jagow.
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Ref.
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Febs Lett, 1987,
219,
161-168.
[DOI no: ]
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PubMed id
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Figure 1.
Fig. 1. Amino acid of the Rieske iron ulfur protein and of the fragments used for sequence determination.
Sequenced parts f te fragments are indicated by solid lines. Broke lines, standing for the parts that were not
sequenced, help to indicate the total length of the fragments used. Arrows indicate the amino acid residues obtained
by cleavage with carboxypeptidase C. N-T, N-terminal sequence; Ac acidolytic fragments; CB, cyanogen bromide
fragments; E, fragments from digestion with Staphylococcus aureus protease V8; K, fragments from digestion with
endoprotinase Lys-C.
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Figure 2.
GE
VKAMSSIFVDVSAvEVGTQLTVKWRGKPVFIRRRDEKDIELARSVPLGALRDTSAENANKPG
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The above figures are
reproduced from the cited reference
with permission from the Federation of European Biochemical Societies
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