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PDBsum entry 1feh
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Oxidoreductase
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PDB id
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1feh
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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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X-Ray crystal structure of the fe-Only hydrogenase (cpi) from clostridium pasteurianum to 1.8 angstrom resolution.
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Authors
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J.W.Peters,
W.N.Lanzilotta,
B.J.Lemon,
L.C.Seefeldt.
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Ref.
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Science, 1998,
282,
1853-1858.
[DOI no: ]
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PubMed id
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Abstract
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A three-dimensional structure for the monomeric iron-containing hydrogenase
(CpI) from Clostridium pasteurianum was determined to 1.8 angstrom resolution by
x-ray crystallography using multiwavelength anomalous dispersion (MAD) phasing.
CpI, an enzyme that catalyzes the two-electron reduction of two protons to yield
dihydrogen, was found to contain 20 gram atoms of iron per mole of protein,
clusters. The probable active-site cluster,
previously termed the H-cluster, was found to be an unexpected arrangement of
cubane subcluster covalently bridged by a
subcluster
both exist with an octahedral coordination geometry and are bridged to each
other by three non-protein atoms, assigned as two sulfide atoms and one carbonyl
or cyanide molecule. This structure provides insights into the mechanism of
cluster
structure and function in biological systems.
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Figure 3.
Fig. 3. (A) Topology diagram of the [2Fe-2S]-containing FS2
domain in a side-by-side comparison with the [2Fe-2S] ferredoxin
from Chorella fusca. The proteins are shown from the same
relative perspective, with the FS2 domain shown in purple and
the C. fusca ferredoxin shown in orange. The [2Fe-2S] cluster is
shown as a space-filling model (colors as in Fig. 1A). (B)
Topology diagram of the 2-[4Fe-4S]-containing FS4A-FS4B domain
in a side-by-side comparison with the 2-[4Fe-4S] ferredoxin from
Chromatium vinosum. The proteins are shown from the same
relative perspective, with the FS4A-FS4B domain shown in green
and the C. vinosum ferredoxin shown in orange. The [4Fe-4S]
clusters are shown as space-filling models. (C) Topology diagram
of the [4Fe-4S]-containing FS4C domain, showing the location and
composition of the four coordinating ligands His94, Cys98,
Cys101, and Cys107.
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Figure 5.
Fig. 5. Stereo view of selected amino acid residues in the
polypeptide environment of the [2Fe] subcluster of HC (colors as
in Fig. 2). The [4Fe-4S] subcluster and associated ligand are
included to provide the proper perspective and are indicated in
light gray. C, Cys; F, Phe; K, Lys; S, Ser; M, Met.
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The above figures are
reprinted
by permission from the AAAs:
Science
(1998,
282,
1853-1858)
copyright 1998.
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