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PDBsum entry 1d4d
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Oxidoreductase
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PDB id
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1d4d
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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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Structure and mechanism of the flavocytochrome c fumarate reductase of shewanella putrefaciens mr-1.
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Authors
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D.Leys,
A.S.Tsapin,
K.H.Nealson,
T.E.Meyer,
M.A.Cusanovich,
J.J.Van beeumen.
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Ref.
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Nat Struct Biol, 1999,
6,
1113-1117.
[DOI no: ]
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PubMed id
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Abstract
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Fumarate respiration is one of the most widespread types of anaerobic
respiration. The soluble fumarate reductase of Shewanella putrefaciens MR-1 is a
periplasmic tetraheme flavocytochrome c. The crystal structures of the enzyme
were solved to 2.9 A for the uncomplexed form and to 2.8 A and 2.5 A for the
fumarate and the succinate-bound protein, respectively. The structures reveal a
flexible capping domain linked to the FAD-binding domain. A catalytic mechanism
for fumarate reduction based on the structure of the complexed protein is
proposed. The mechanism for the reverse reaction is a model for the homologous
succinate dehydrogenase (complex II) of the respiratory chain. In
flavocytochrome c fumarate reductase, all redox centers are in van der Waals
contact with one another, thus providing an efficient conduit of electrons from
the hemes via the FAD to fumarate.
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Figure 1.
Figure 1. Protein fold of the soluble fumarate reductase.
a,b, Ribbon representation of fumarate reductase; molecule A of
the orthorhombic crystal form is depicted. The cytochrome domain
I is in orange and domains II, III and IV are in light blue,
dark blue and green, respectively. The orientation in (b) is
rotated 90° counter-clockwise horizontally and 90°
clockwise along the vertical axis with respect to (a). Both
figures were made using Molscript^30 and Raster3D^31. c,
Superposition of the structures of fumarate reductase in the
tetragonal form (green) and the orthorhombic crystal (molecule
A, red; molecule D, blue) using the C  coordinates
of the FAD binding domain as the reference (figure generated
using TURBO-FRODO^28). The view is approximately along the axis
of rotation around the double hinge (see text) situated near
residue 503. For clarity, only domains I, II and IV in molecule
D of the orthorhombic crystal form (black lines) are shown.
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Figure 3.
Figure 3. Stereo representation of the redox centers in fumarate
reductase. Hemes are colored yellow (except the iron atoms,
which are orange), FAD blue and the substrate green. The figure
was prepared using Molscript^30 and Raster3D^31.
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The above figures are
reprinted
by permission from Macmillan Publishers Ltd:
Nat Struct Biol
(1999,
6,
1113-1117)
copyright 1999.
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