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PDBsum entry 4zkx
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Oxidoreductase
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PDB id
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4zkx
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PDB id:
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| Name: |
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Oxidoreductase
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Title:
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Crystal structure of the pmftn variant e44q soaked in iron (5 min)
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Structure:
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Ferritin. Chain: a, d, b, c, e, f, g, h. Engineered: yes. Mutation: yes
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Source:
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Pseudo-nitzschia multiseries. Organism_taxid: 37319. Gene: ftn. Expressed in: escherichia coli. Expression_system_taxid: 469008.
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Resolution:
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1.80Å
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R-factor:
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0.169
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R-free:
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0.201
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Authors:
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S.Pfaffen,M.E.P.Murphy
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Key ref:
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S.Pfaffen
et al.
(2015).
A Diatom Ferritin Optimized for Iron Oxidation but Not Iron Storage.
J Biol Chem,
290,
28416-28427.
PubMed id:
DOI:
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Date:
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30-Apr-15
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Release date:
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30-Sep-15
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PROCHECK
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Headers
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References
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B6DMH6
(B6DMH6_PSEMU) -
Ferritin (Fragment) from Pseudo-nitzschia multiseries
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Seq:
Struc:
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230 a.a.
157 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 2 residue positions (black
crosses)
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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 Biol Chem
290:28416-28427
(2015)
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PubMed id:
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A Diatom Ferritin Optimized for Iron Oxidation but Not Iron Storage.
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S.Pfaffen,
J.M.Bradley,
R.Abdulqadir,
M.R.Firme,
G.R.Moore,
N.E.Le Brun,
M.E.Murphy.
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ABSTRACT
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Ferritin from the marine pennate diatom Pseudo-nitzschia multiseries (PmFTN)
plays a key role in sustaining growth in iron-limited ocean environments. The
di-iron catalytic ferroxidase center of PmFTN (sites A and B) has a nearby third
iron site (site C) in an arrangement typically observed in prokaryotic
ferritins. Here we demonstrate that Glu-44, a site C ligand, and Glu-130, a
residue that bridges iron bound at sites B and C, limit the rate of
post-oxidation reorganization of iron coordination and the rate at which Fe(3+)
exits the ferroxidase center for storage within the mineral core. The latter, in
particular, severely limits the overall rate of iron mineralization. Thus, the
diatom ferritin is optimized for initial Fe(2+) oxidation but not for
mineralization, pointing to a role for this protein in buffering iron
availability and facilitating iron-sparing rather than only long-term iron
storage.
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Links
