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PDBsum entry 1gx7
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Oxidoreductase
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PDB id
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1gx7
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Contents |
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371 a.a.
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88 a.a.
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107 a.a.
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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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The cytochrome c3-[Fe]-Hydrogenase electron-Transfer complex: structural model by nmr restrained docking.
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Authors
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L.Elantak,
X.Morelli,
O.Bornet,
C.Hatchikian,
M.Czjzek,
A.Dolla,
F.Guerlesquin.
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Ref.
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FEBS Lett, 2003,
548,
1-4.
[DOI no: ]
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PubMed id
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Abstract
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Cytochrome c(3) (M(r) 13000) is a low redox potential cytochrome specific of the
anaerobic metabolism in sulfate-reducing bacteria. This tetrahemic cytochrome is
an intermediate between the [Fe]-hydrogenase and the cytochrome Hmc in
Desulfovibrio vulgaris Hildenborough strain. The present work describes the
structural model of the cytochrome c(3)-[Fe]-hydrogenase complex obtained by
nuclear magnetic resonance restrained docking. This model connects the distal
cluster of the [Fe]-hydrogenase to heme 4 of the cytochrome, the same heme found
in the interaction with cytochrome Hmc. This result gives evidence that
cytochrome c(3) is an electron shuttle between the periplasmic hydrogenase and
the Hmc membrane-bound complex.
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Figure 3.
Fig. 3. A: Ribbon representation of the best representative
structure of the [Fe]-hydrogenase–cytochrome c[3] complex. The
[Fe]-hydrogenase is the left polypeptide chain, the large
subunit is colored in beige; the small subunit is colored in
yellow and the ferredoxin-like domain in blue, the iron
clusters are in green. Cytochrome c[3] is the right polypeptide
chain colored in blue, the heme groups are in red. B: Zoom-in
view of the interface region, highlighting the residues involved
in interatomic contacts within the cytochrome
c[3]–[Fe]-hydrogenase complex. Heme 4 and cytochrome c[3]
residues are labeled in red, distal [4Fe–4S] cluster and
residues of [Fe]-hydrogenase are labeled in green.
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Figure 4.
Fig. 4. A possible mechanism for ALAD in which both A- and
P-side substrates form Schiff bases with the enzyme.
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The above figures are
reprinted
by permission from the Federation of European Biochemical Societies:
FEBS Lett
(2003,
548,
1-4)
copyright 2003.
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