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PDBsum entry 1e08
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Contents |
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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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Structural model of the fe-Hydrogenase/cytochrome c553 complex combining transverse relaxation-Optimized spectroscopy experiments and soft docking calculations.
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Authors
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X.Morelli,
M.Czjzek,
C.E.Hatchikian,
O.Bornet,
J.C.Fontecilla-Camps,
N.P.Palma,
J.J.Moura,
F.Guerlesquin.
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Ref.
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J Biol Chem, 2000,
275,
23204-23210.
[DOI no: ]
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PubMed id
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Abstract
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Fe-hydrogenase is a 54-kDa iron-sulfur enzyme essential for hydrogen cycling in
sulfate-reducing bacteria. The x-ray structure of Desulfovibrio desulfuricans
Fe-hydrogenase has recently been solved, but structural information on the
recognition of its redox partners is essential to understand the
structure-function relationships of the enzyme. In the present work, we have
obtained a structural model of the complex of Fe-hydrogenase with its redox
partner, the cytochrome c(553), combining docking calculations and NMR
experiments. The putative models of the complex demonstrate that the small
subunit of the hydrogenase has an important role in the complex formation with
the redox partner; 50% of the interacting site on the hydrogenase involves the
small subunit. The closest contact between the redox centers is observed between
Cys-38, a ligand of the distal cluster of the hydrogenase and Cys-10, a ligand
of the heme in the cytochrome. The electron pathway from the distal cluster of
the Fe-hydrogenase to the heme of cytochrome c(553) was investigated using the
software Greenpath and indicates that the observed cysteine/cysteine contact has
an essential role. The spatial arrangement of the residues on the interface of
the complex is very similar to that already described in the
ferredoxin-cytochrome c(553) complex, which therefore, is a very good model for
the interacting domain of the Fe-hydrogenase-cytochrome c(553).
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Figure 3.
Fig. 3. A, 1H and 15N chemical shift variations of
cytochrome c[553] NH groups observed in TROSY experiments. B,
mapping of the hydrogenase interacting site on the cytochrome
c[553], obtained by heteronuclear experiments. In the top
figure, the heme is colored in red, the NH groups whose
resonances undergo chemical shift variations are in green,
unassigned residues are in blue, and unaffected residues are in
white. The bottom figure shows a 180° rotation along the x
axis and represents the "back side" of the molecule.
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Figure 5.
Fig. 5. Model of fam1 solution 3 using Grasp software. A,
ribbon model of the cytochrome c[553]-hydrogenase complex. For
hydrogenase, the ferredoxin-like domain is in green, the large
subunit is in blue, and the small subunit is in yellow. The
cytochrome c[553] is in red. B, view of interface in the
cytochrome c[553]-ferredoxin complex (a) and in the cytochrome
c[553]-hydrogenase complex (b).
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The above figures are
reprinted
by permission from the ASBMB:
J Biol Chem
(2000,
275,
23204-23210)
copyright 2000.
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Secondary reference #1
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Title
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Heteronuclear nmr and soft docking: an experimental approach for a structural model of the cytochrome c553-Ferredoxin complex.
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Authors
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X.Morelli,
A.Dolla,
M.Czjzek,
P.N.Palma,
F.Blasco,
L.Krippahl,
J.J.Moura,
F.Guerlesquin.
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Ref.
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Biochemistry, 2000,
39,
2530-2537.
[DOI no: ]
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PubMed id
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