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PDBsum entry 1e6e
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Oxidoreductase
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PDB id
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1e6e
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Contents |
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457 a.a.
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113 a.a.
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106 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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Adrenodoxin reductase-Adrenodoxin complex structure suggests electron transfer path in steroid biosynthesis.
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Authors
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J.J.Müller,
A.Lapko,
G.Bourenkov,
K.Ruckpaul,
U.Heinemann.
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Ref.
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J Biol Chem, 2001,
276,
2786-2789.
[DOI no: ]
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PubMed id
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Abstract
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The steroid hydroxylating system of adrenal cortex mitochondria consists of the
membrane-attached NADPH-dependent adrenodoxin reductase (AR), the soluble
one-electron transport protein adrenodoxin (Adx), and a membrane-integrated
cytochrome P450 of the CYP11 family. In the 2.3-A resolution crystal structure
of the Adx.AR complex, 580 A(2) of partly polar surface are buried. Main
interaction sites are centered around Asp(79), Asp(76), Asp(72), and Asp(39) of
Adx and around Arg(211), Arg(240), Arg(244), and Lys(27) of AR, respectively. In
particular, the region around Asp(39) defines a new protein interaction site for
Adx, similar to those found in plant and bacterial ferredoxins. Additional
contacts involve the electron transfer region between the redox centers of AR
and Adx and C-terminal residues of Adx. The Adx residues Asp(113) to Arg(115)
adopt 3(10)-helical conformation and engage in loose intermolecular contacts
within a deep cleft of AR. Complex formation is accompanied by a slight domain
rearrangement in AR. The [2Fe-2S] cluster of Adx and the isoalloxazine rings of
FAD of AR are 10 A apart suggesting a possible electron transfer route between
these redox centers. The AR.Adx complex represents the first structure of a
biologically relevant complex between a ferredoxin and its reductase.
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Figure 1.
Fig. 1. Crystal structure of the AR·Adx complex.
AR-Adx contacts occur at the primary and secondary interaction
regions and the region between the [2Fe-2S] cluster of Adx and
the isoalloxazine ring of the FAD of AR. C-terminal residues of
Adx are also in contact with AR. The side chains of some
residues involved in polar AR-Adx interactions are displayed.
For close-ups of the contact sites see Figs. 3 and 4. The brown
triangle marks the position of Adx Lys66 and the green marks AR
Glu4, both residues maintaining another cross-link reported
recently (11, 12). Figure was produced with MOLSCRIPT (17).
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Figure 4.
Fig. 4. Electron transfer region between the [2Fe-2S]
cluster of Adx and the FAD moiety of AR. The hypothetical
electron pathway shown in red was calculated with the program
HARLEM (31). Red dotted lines mark through-space electron jumps.
The AR-Adx interface is stabilized by hydrogen bonds (blue
dotted lines) and van der Waals contacts. Residues are labeled
black for AR and red for Adx. The blue spheres are water
molecules.
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The above figures are
reprinted
by permission from the ASBMB:
J Biol Chem
(2001,
276,
2786-2789)
copyright 2001.
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Secondary reference #1
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Title
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X-Ray structure of bovine adrenodoxin reductase - Adrenodoxin complex at 2.5 a resolution: the first three-Dimensional structure of a complex of two components of the steroidogenic electron transport system in adrenal cortex mitochondria
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Authors
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J.J.Mueller,
A.Lapko,
G.Bourenkov,
E.C.Mueller,
A.Otto,
K.Ruckpaul,
U.Heinemann.
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Ref.
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TO BE PUBLISHED ...
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Secondary reference #2
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Title
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Preparation and crystallization of a cross-Linked complex of bovine adrenodoxin and adrenodoxin reductase.
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Authors
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A.Lapko,
A.Müller,
O.Heese,
K.Ruckpaul,
U.Heinemann.
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Ref.
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Proteins, 1997,
28,
289-292.
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PubMed id
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