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PDBsum entry 1dcd
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Electron transport
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PDB id
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1dcd
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Contents |
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* Residue conservation analysis
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DOI no:
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Protein Sci
8:1536-1545
(1999)
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PubMed id:
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Structural studies by X-ray diffraction on metal substituted desulforedoxin, a rubredoxin-type protein.
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M.Archer,
A.L.Carvalho,
S.Teixeira,
I.Moura,
J.J.Moura,
F.Rusnak,
M.J.Romão.
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ABSTRACT
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Desulforedoxin (Dx), isolated from the sulfate reducing bacterium Desulfovibrio
gigas, is a small homodimeric (2 x 36 amino acids) protein. Each subunit
contains a high-spin iron atom tetrahedrally bound to four cysteinyl sulfur
atoms, a metal center similar to that found in rubredoxin (Rd) type proteins.
The simplicity of the active center in Dx and the possibility of replacing the
iron by other metals make this protein an attractive case for the
crystallographic analysis of metal-substituted derivatives. This study extends
the relevance of Dx to the bioinorganic chemistry field and is important to
obtain model compounds that can mimic the four sulfur coordination of metals in
biology. Metal replacement experiments were carried out by reconstituting the
apoprotein with In3+, Ga3+, Cd2+, Hg2+, and Ni2+ salts. The In3+ and Ga3+
derivatives are isomorphous with the iron native protein; whereas Cd2+, Hg2+,
and Ni2+ substituted Dx crystallized under different experimental conditions,
yielding two additional crystal morphologies; their structures were determined
by the molecular replacement method. A comparison of the three-dimensional
structures for all metal derivatives shows that the overall secondary and
tertiary structures are maintained, while some differences in metal coordination
geometry occur, namely, bond lengths and angles of the metal with the sulfur
ligands. These data are discussed in terms of the entatic state theory.
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Literature references that cite this PDB file's key reference
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PubMed id
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Reference
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J.Hong,
O.A.Kharenko,
and
M.Y.Ogawa
(2006).
Incorporating electron-transfer functionality into synthetic metalloproteins from the bottom-up.
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Inorg Chem,
45,
9974-9984.
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T.Santos-Silva,
J.Trincão,
A.L.Carvalho,
C.Bonifácio,
F.Auchère,
P.Raleiras,
I.Moura,
J.J.Moura,
and
M.J.Romão
(2006).
The first crystal structure of class III superoxide reductase from Treponema pallidum.
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J Biol Inorg Chem,
11,
548-558.
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PDB code:
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M.Maher,
M.Cross,
M.C.Wilce,
J.M.Guss,
and
A.G.Wedd
(2004).
Metal-substituted derivatives of the rubredoxin from Clostridium pasteurianum.
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Acta Crystallogr D Biol Crystallogr,
60,
298-303.
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PDB codes:
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B.J.Goodfellow,
S.G.Nunes,
F.Rusnak,
I.Moura,
C.Ascenso,
J.J.Moura,
B.F.Volkman,
and
J.L.Markley
(2002).
Zinc-substituted Desulfovibrio gigas desulforedoxins: resolving subunit degeneracy with nonsymmetric pseudocontact shifts.
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Protein Sci,
11,
2464-2470.
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The most recent references are shown first.
Citation data come partly from CiteXplore and partly
from an automated harvesting procedure. Note that this is likely to be
only a partial list as not all journals are covered by
either method. However, we are continually building up the citation data
so more and more references will be included with time.
Where a reference describes a PDB structure, the PDB
code is
shown on the right.
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Links
