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PDBsum entry 1s3q
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Metal binding protein
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PDB id
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1s3q
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* Residue conservation analysis
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PDB id:
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Metal binding protein
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Title:
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Crystal structures of a novel open pore ferritin from the hyperthermophilic archaeon archaeoglobus fulgidus
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Structure:
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Ferritin. Chain: a, b, c, d, e, f, g, h, i, j, k, l. Engineered: yes
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Source:
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Archaeoglobus fulgidus. Organism_taxid: 2234. Gene: ftn. Expressed in: escherichia coli. Expression_system_taxid: 562.
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Biol. unit:
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24mer (from PDB file)
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Resolution:
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2.10Å
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R-factor:
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0.181
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R-free:
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0.218
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Authors:
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E.Johnson,D.Cascio,M.Sawaya,I.Schroeder
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Key ref:
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E.Johnson
et al.
(2005).
Crystal structures of a tetrahedral open pore ferritin from the hyperthermophilic archaeon Archaeoglobus fulgidus.
Structure,
13,
637-648.
PubMed id:
DOI:
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Date:
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13-Jan-04
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Release date:
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12-Apr-05
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PROCHECK
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Headers
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References
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O29424
(O29424_ARCFU) -
Ferritin, putative from Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16)
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Seq: Struc:
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173 a.a.
162 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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DOI no:
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Structure
13:637-648
(2005)
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PubMed id:
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Crystal structures of a tetrahedral open pore ferritin from the hyperthermophilic archaeon Archaeoglobus fulgidus.
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E.Johnson,
D.Cascio,
M.R.Sawaya,
M.Gingery,
I.Schröder.
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ABSTRACT
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Ferritins are known as important iron storage/detoxification proteins and are
widely found in living organisms. This report details the 2.1 A resolution
native and 2.7 A resolution iron bound structures of the ferritin from the
hyperthermophilic Archaeon Archaeoglobus fulgidus, and represents the first
structure of a ferritin from an archaeon, or a hyperthermophilic organism. The
A. fulgidus ferritin (AfFtn) monomer has a high degree of structural similarity
with archetypal ferritins from E. coli and humans, but the AfFtn quaternary
structure is novel; 24 subunits assemble into a shell having tetrahedral (2-3)
rather than the canonical octahedral (4-3-2) symmetry of archetypal ferritins.
The difference in assembly opens four large (approximately 45 A) pores in the
AfFtn shell. Two nonconservative amino acid substitutions may be critical for
stabilizing the tetrahedral form.
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Selected figure(s)
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Figure 2.
Figure 2. Subunit Structure of the AfFtn (A) A cartoon
ribbon representation of the AfFtn monomer (native structure)
showing the location of the two bound Zn2+ ions. The model is
colored green except for residues which are identical in the
AfFtn, EcFtnA, and HuHf which are colored blue or red (red
indicates conserved ferroxidase center residues). (B)
Tube-style cartoon representation of AfFtn structure (green)
with EcFtnA (blue) structure superimposed (rmsd 0.849 Å, 158
C^a). The orientation of the AfFtn molecule is identical to that
in (A). (C) Structural superpositioning of AfFtn (green),
and HuHf structures (rmsd 1.09 Å, 157 C^a). Images created using
PYMOL.
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The above figure is
reprinted
by permission from Cell Press:
Structure
(2005,
13,
637-648)
copyright 2005.
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Figure was
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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P.Ceci,
E.Forte,
G.Di Cecca,
M.Fornara,
and
E.Chiancone
(2011).
The characterization of Thermotoga maritima ferritin reveals an unusual subunit dissociation behavior and efficient DNA protection from iron-mediated oxidative stress.
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Extremophiles,
15,
431-439.
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B.Sana,
E.Johnson,
K.Sheah,
C.L.Poh,
and
S.Lim
(2010).
Iron-based ferritin nanocore as a contrast agent.
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Biointerphases,
5,
FA48-FA52.
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K.Honarmand Ebrahimi,
P.L.Hagedoorn,
J.A.Jongejan,
and
W.R.Hagen
(2009).
Catalysis of iron core formation in Pyrococcus furiosus ferritin.
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J Biol Inorg Chem,
14,
1265-1274.
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C.L.Lawson,
S.Dutta,
J.D.Westbrook,
K.Henrick,
and
H.M.Berman
(2008).
Representation of viruses in the remediated PDB archive.
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Acta Crystallogr D Biol Crystallogr,
64,
874-882.
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C.S.Kaddis,
S.H.Lomeli,
S.Yin,
B.Berhane,
M.I.Apostol,
V.A.Kickhoefer,
L.H.Rome,
and
J.A.Loo
(2007).
Sizing large proteins and protein complexes by electrospray ionization mass spectrometry and ion mobility.
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J Am Soc Mass Spectrom,
18,
1206-1216.
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J.Tatur,
W.R.Hagen,
and
P.M.Matias
(2007).
Crystal structure of the ferritin from the hyperthermophilic archaeal anaerobe Pyrococcus furiosus.
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J Biol Inorg Chem,
12,
615-630.
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PDB codes:
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J.Tatur,
P.L.Hagedoorn,
M.L.Overeijnder,
and
W.R.Hagen
(2006).
A highly thermostable ferritin from the hyperthermophilic archaeal anaerobe Pyrococcus furiosus.
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Extremophiles,
10,
139-148.
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P.M.Matias,
J.Tatur,
M.A.Carrondo,
and
W.R.Hagen
(2005).
Crystallization and preliminary X-ray characterization of a ferritin from the hyperthermophilic archaeon and anaerobe Pyrococcus furiosus.
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Acta Crystallogr Sect F Struct Biol Cryst Commun,
61,
503-506.
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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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}
}
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