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PDBsum entry 4xkt
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Metal binding protein
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PDB id
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4xkt
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PDB id:
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Metal binding protein
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Title:
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E coli bfr variant y149f
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Structure:
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Bacterioferritin. Chain: a, b, c, d, e, f, g, h, i, j, k, l. Engineered: yes. Mutation: yes
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Source:
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Escherichia coli. Organism_taxid: 562. Gene: bfr, bn1008_2995, bn17_32701, bu34_11470, bu65_02845, bu66_00425, bu67_22375, bu68_21080, bu69_14600, cf57_02675, cf61_03435, do98_13405, dp79_03550, echms174_03989, ecrv308_03369, eh62_04010, eh63_09485, eh64_04335, eh65_17065, eh66_25435, el75_0360, el77_0399, el78_0411, el79_0379, el80_0371, ep08_09090, gr02_14320, gr05_21335, gr06_21735, kv39_17170, lf82_0224, pgd_00550.
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Resolution:
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1.82Å
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R-factor:
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0.169
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R-free:
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0.206
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Authors:
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J.M.Bradley,A.M.Hemmings,N.E.Le Brun
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Key ref:
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J.M.Bradley
et al.
(2015).
Three Aromatic Residues are Required for Electron Transfer during Iron Mineralization in Bacterioferritin.
Angew Chem Int Ed Engl,
54,
14763-14767.
PubMed id:
DOI:
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Date:
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12-Jan-15
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Release date:
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16-Dec-15
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PROCHECK
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Headers
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References
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P0ABD3
(BFR_ECOLI) -
Bacterioferritin from Escherichia coli (strain K12)
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Seq:
Struc:
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158 a.a.
158 a.a.*
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Key: |
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PfamA domain |
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Secondary structure |
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CATH domain |
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*
PDB and UniProt seqs differ
at 1 residue position (black
cross)
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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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Angew Chem Int Ed Engl
54:14763-14767
(2015)
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PubMed id:
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Three Aromatic Residues are Required for Electron Transfer during Iron Mineralization in Bacterioferritin.
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J.M.Bradley,
D.A.Svistunenko,
T.L.Lawson,
A.M.Hemmings,
G.R.Moore,
N.E.Le Brun.
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ABSTRACT
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Ferritins are iron storage proteins that overcome the problems of toxicity and
poor bioavailability of iron by catalyzing iron oxidation and mineralization
through the activity of a diiron ferroxidase site. Unlike in other ferritins,
the oxidized di-Fe(3+) site of Escherichia coli bacterioferritin (EcBFR) is
stable and therefore does not function as a conduit for the transfer of Fe(3+)
into the storage cavity, but instead acts as a true catalytic cofactor that
cycles its oxidation state while driving Fe(2+) oxidation in the cavity. Herein,
we demonstrate that EcBFR mineralization depends on three aromatic residues near
the diiron site, Tyr25, Tyr58, and Trp133, and that a transient radical is
formed on Tyr25. The data indicate that the aromatic residues, together with a
previously identified inner surface iron site, promote mineralization by
ensuring the simultaneous delivery of two electrons, derived from Fe(2+)
oxidation in the BFR cavity, to the di-ferric catalytic site for safe reduction
of O2 .
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Links
