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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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References listed in PDB file
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Key reference
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Title
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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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Authors
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L.Toussaint,
L.Bertrand,
L.Hue,
R.R.Crichton,
J.P.Declercq.
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Ref.
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J Mol Biol, 2007,
365,
440-452.
[DOI no: ]
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PubMed id
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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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The above figures are
reprinted
by permission from Elsevier:
J Mol Biol
(2007,
365,
440-452)
copyright 2007.
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