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PDBsum entry 2clu
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Oxidoreductase
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PDB id
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2clu
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Contents |
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* Residue conservation analysis
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Enzyme class:
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E.C.1.16.3.1
- ferroxidase.
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Reaction:
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4 Fe2+ + O2 + 4 H+ = 4 Fe3+ + 2 H2O
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4
×
Fe(2+)
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+
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O2
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+
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4
×
H(+)
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=
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4
×
Fe(3+)
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+
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2
×
H2O
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Cofactor:
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Cu cation
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Molecule diagrams generated from .mol files obtained from the
KEGG ftp site
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DOI no:
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J Mol Biol
365:440-452
(2007)
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PubMed id:
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High-resolution X-ray structures of human apoferritin H-chain mutants correlated with their activity and metal-binding sites.
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L.Toussaint,
L.Bertrand,
L.Hue,
R.R.Crichton,
J.P.Declercq.
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ABSTRACT
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Ferritins are a family of proteins distributed widely in nature. In bacterial,
plant, and animal cells, ferritin appears to serve as a soluble, bioavailable,
and non-toxic form of iron provider. Ferritins from animal sources are
heteropolymers composed of two types of subunit, H and L, which differ mainly by
the presence (H) or absence (L) of active ferroxidase centres. We report the
crystallographic structures of four human H apoferritin variants at a resolution
of up to 1.5 Angstrom. Crystal derivatives using Zn(II) as redox-stable
alternative for Fe(II), allows us to characterize the different metal-binding
sites. The ferroxidase centre, which is composed of sites A and B, binds metal
with a preference for the A site. In addition, distinct Zn(II)-binding sites
were found in the 3-fold axes, 4-fold axes and on the cavity surface near the
ferroxidase centre. To study the importance of the distance of the two metal
atoms in the ferroxidase centre, single and double replacement of glutamate 27
(site A) and glutamate 107 (site B), the two axial ligands, by aspartate
residues have been carried out. The consequences for metal binding and the
correlation with Fe(II) oxidation rates are discussed.
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Selected figure(s)
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The above figures are
reprinted
by permission from Elsevier:
J Mol Biol
(2007,
365,
440-452)
copyright 2007.
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Figures were
selected
by an automated process.
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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.Deng,
X.Liao,
J.Hu,
X.Leng,
J.Cheng,
and
G.Zhao
(2010).
Purification and characterization of new phytoferritin from black bean (Phaseolus vulgaris L.) seed.
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J Biochem,
147,
679-688.
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K.Honarmand Ebrahimi,
P.L.Hagedoorn,
and
W.R.Hagen
(2010).
Inhibition and stimulation of formation of the ferroxidase center and the iron core in Pyrococcus furiosus ferritin.
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J Biol Inorg Chem,
15,
1243-1253.
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T.Masuda,
F.Goto,
T.Yoshihara,
and
B.Mikami
(2010).
Crystal structure of plant ferritin reveals a novel metal binding site that functions as a transit site for metal transfer in ferritin.
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J Biol Chem,
285,
4049-4059.
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PDB codes:
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L.Toussaint,
M.G.Cuypers,
L.Bertrand,
L.Hue,
C.V.Romão,
L.M.Saraiva,
M.Teixeira,
W.Meyer-Klaucke,
M.C.Feiters,
and
R.R.Crichton
(2009).
Comparative Fe and Zn K-edge X-ray absorption spectroscopic study of the ferroxidase centres of human H-chain ferritin and bacterioferritin from Desulfovibrio desulfuricans.
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J Biol Inorg Chem,
14,
35-49.
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R.C.Binning,
and
D.E.Bacelo
(2009).
Computational modeling of the dizinc-ferroxidase complex of human H ferritin: direct comparison of the density functional theory calculated and experimental structures.
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J Biol Inorg Chem,
14,
1199-1208.
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E.L.MacKenzie,
K.Iwasaki,
and
Y.Tsuji
(2008).
Intracellular iron transport and storage: from molecular mechanisms to health implications.
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Antioxid Redox Signal,
10,
997.
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F.Bou-Abdallah,
G.Zhao,
G.Biasiotto,
M.Poli,
P.Arosio,
and
N.D.Chasteen
(2008).
Facilitated diffusion of iron(II) and dioxygen substrates into human H-chain ferritin. A fluorescence and absorbance study employing the ferroxidase center substitution Y34W.
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J Am Chem Soc,
130,
17801-17811.
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H.Havukainen,
S.Haataja,
A.Kauko,
A.T.Pulliainen,
A.Salminen,
T.Haikarainen,
J.Finne,
and
A.C.Papageorgiou
(2008).
Structural basis of the zinc- and terbium-mediated inhibition of ferroxidase activity in Dps ferritin-like proteins.
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Protein Sci,
17,
1513-1521.
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PDB codes:
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J.K.Schwartz,
X.S.Liu,
T.Tosha,
E.C.Theil,
and
E.I.Solomon
(2008).
Spectroscopic definition of the ferroxidase site in M ferritin: comparison of binuclear substrate vs cofactor active sites.
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J Am Chem Soc,
130,
9441-9450.
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T.Tosha,
M.R.Hasan,
and
E.C.Theil
(2008).
The ferritin Fe2 site at the diiron catalytic center controls the reaction with O2 in the rapid mineralization pathway.
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Proc Natl Acad Sci U S A,
105,
18182-18187.
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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
codes are
shown on the right.
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Links
