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Electron transport
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PDB id
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1b71
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* Residue conservation analysis
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Gene Ontology (GO) functional annotation
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Cellular component
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cellular_component
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2 terms
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Biological process
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oxidation-reduction process
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3 terms
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Biochemical function
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oxidoreductase activity
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4 terms
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DOI no:
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Nat Struct Biol
6:308-309
(1999)
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PubMed id:
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Alternative metal-binding sites in rubrerythrin.
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L.C.Sieker,
M.Holmes,
I.Le Trong,
S.Turley,
B.D.Santarsiero,
M.Y.Liu,
J.LeGall,
R.E.Stenkamp.
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ABSTRACT
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Selected figure(s)
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Figure 1.
Figure 1. a, Difference electron density (|F[o]| - |F[c]|)
for aerobically purified rubrerythrin. Cyan contours are drawn
at 3 .
Orange contours (3 )
are shown for the Bijvoet difference density and indicate the
location of atoms with significant anomalous scattering. Phases
for both maps were calculated for a protein model obtained by
deletion of the iron atoms and water molecules from coordinate
set 1RYT, followed by five cycles of refinement to reduce model
bias. Sites A, B, C and D are labeled in the figure to simplify
the nomenclature and site descriptions in the text. Figure drawn
with XtalView^13. b, Difference density (|F[o]| - |F[c]|) for
uranyl-soaked crystals superposed on the phasing model obtained
as described for (a). Cyan contours are drawn at 3 .
Orange contours (3 )
and yellow contours (10 )
are shown for the Bijvoet difference density. Sites labeled as
described for (a). Figure drawn with XtalView^13. c, Stereo view
of the Fe−Zn complex in aerobically purified rubrerythrin.
Figures drawn with MOLSCRIPT^12.
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The above figure is
reprinted
by permission from Macmillan Publishers Ltd:
Nat Struct Biol
(1999,
6,
308-309)
copyright 1999.
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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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M.A.Carrondo,
I.Bento,
P.M.Matias,
and
P.F.Lindley
(2007).
Crystallographic evidence for dioxygen interactions with iron proteins.
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J Biol Inorg Chem, 12,
429-442.
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S.Sacquin-Mora,
and
R.Lavery
(2006).
Investigating the local flexibility of functional residues in hemoproteins.
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Biophys J, 90,
2706-2717.
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M.V.Weinberg,
F.E.Jenney,
X.Cui,
and
M.W.Adams
(2004).
Rubrerythrin from the hyperthermophilic archaeon Pyrococcus furiosus is a rubredoxin-dependent, iron-containing peroxidase.
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J Bacteriol, 186,
7888-7895.
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D.T.Logan,
E.Mulliez,
K.M.Larsson,
S.Bodevin,
M.Atta,
P.E.Garnaud,
B.M.Sjoberg,
and
M.Fontecave
(2003).
A metal-binding site in the catalytic subunit of anaerobic ribonucleotide reductase.
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Proc Natl Acad Sci U S A, 100,
3826-3831.
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PDB code:
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T.Wakagi
(2003).
Sulerythrin, the smallest member of the rubrerythrin family, from a strictly aerobic and thermoacidophilic archaeon, Sulfolobus tokodaii strain 7.
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FEMS Microbiol Lett, 222,
33-37.
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C.M.Gomes,
J.Le Gall,
A.V.Xavier,
and
M.Teixeira
(2001).
Could a diiron-containing four-helix-bundle protein have been a primitive oxygen reductase?
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Chembiochem, 2,
583-587.
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A.Lombardi,
C.M.Summa,
S.Geremia,
L.Randaccio,
V.Pavone,
and
W.F.DeGrado
(2000).
Inaugural article: retrostructural analysis of metalloproteins: application to the design of a minimal model for diiron proteins.
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Proc Natl Acad Sci U S A, 97,
6298-6305.
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PDB code:
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C.V.Romåo,
M.Regalla,
A.V.Xavier,
M.Teixeira,
M.Y.Liu,
and
J.Le Gall
(2000).
A bacterioferritin from the strict anaerobe Desulfovibrio desulfuricans ATCC 27774.
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Biochemistry, 39,
6841-6849.
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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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