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PDBsum entry 1soy
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Unknown function
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PDB id
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1soy
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References listed in PDB file
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Key reference
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Title
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Solution structure of the bacterial frataxin ortholog, Cyay: mapping the iron binding sites.
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Authors
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M.Nair,
S.Adinolfi,
C.Pastore,
G.Kelly,
P.Temussi,
A.Pastore.
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Ref.
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Structure, 2004,
12,
2037-2048.
[DOI no: ]
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PubMed id
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Abstract
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CyaY is the bacterial ortholog of frataxin, a small mitochondrial iron binding
protein thought to be involved in iron sulphur cluster formation. Loss of
frataxin function leads to the neurodegenerative disorder Friedreich's ataxia.
We have solved the solution structure of CyaY and used the structural
information to map iron binding onto the protein surface. Comparison of the
behavior of wild-type CyaY with that of a mutant indicates that specific binding
with a defined stoichiometry does not require aggregation and that the main
binding site, which hosts both Fe(2+) and Fe(3+), occupies a highly anionic
surface of the molecule. This function is conserved across species since the
corresponding region of human frataxin is also able to bind iron, albeit with
weaker affinity. The presence of secondary binding sites on CyaY, but not on
frataxin, hints at a possible polymerization mechanism. We suggest mutations
that may provide further insights into the frataxin function.
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Figure 1.
Figure 1. Solution Structure of CyaY and Comparison with
the Crystal Structure and the Human Ortholog(A) A set of 20
energy-minimized conformers of bacterial frataxin CyaY
superposed on the average structure (shown in red).(B) Average
NMR structure showing the N- and C-terminal a helices packed
against a six-stranded b sheet. The N and C termini are also
indicated.(C) Pairwise superposition of the corresponding NMR
(in green) and crystallographic (1ew4, in blue) structures of
CyaY is shown.(D) Structural comparison of the NMR (1ly7, in
green) and the crystal (1dlx, in green) structures of
hfra(91-210) (in blue) using the same orientation as in (C).
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The above figure is
reprinted
by permission from Cell Press:
Structure
(2004,
12,
2037-2048)
copyright 2004.
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