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PDBsum entry 2jd8
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Metal transport
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PDB id
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2jd8
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References listed in PDB file
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Key reference
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Title
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Crystal structure of the ferritin from the hyperthermophilic archaeal anaerobe pyrococcus furiosus.
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Authors
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J.Tatur,
W.R.Hagen,
P.M.Matias.
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Ref.
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J Biol Inorg Chem, 2007,
12,
615-630.
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PubMed id
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Abstract
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The crystal structure of the ferritin from the archaeon, hyperthermophile and
anaerobe Pyrococcus furiosus (PfFtn) is presented. While many ferritin
structures from bacteria to mammals have been reported, until now only one was
available from archaea, the ferritin from Archaeoglobus fulgidus (AfFtn). The
PfFtn 24-mer exhibits the 432 point-group symmetry that is characteristic of
most ferritins, which suggests that the 23 symmetry found in the previously
reported AfFtn is not a common feature of archaeal ferritins. Consequently, the
four large pores that were found in AfFtn are not present in PfFtn. The
structure has been solved by molecular replacement and refined at 2.75-Angstrom
resolution to R = 0.195 and R(free) = 0.247. The ferroxidase center of the
aerobically crystallized ferritin contains one iron at site A and shows sites B
and C only upon iron or zinc soaking. Electron paramagnetic resonance studies
suggest this iron depletion of the native ferroxidase center to be a result of a
complexation of iron by the crystallization salt. The extreme thermostability of
PfFtn is compared with that of eight structurally similar ferritins and is
proposed to originate mostly from the observed high number of intrasubunit
hydrogen bonds. A preservation of the monomer fold, rather than the 24-mer
assembly, appears to be the most important factor that protects the ferritin
from inactivation by heat.
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Secondary reference #1
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Title
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Crystallization and preliminary X-Ray characterization of a ferritin from the hyperthermophilic archaeon and anaerobe pyrococcus furiosus.
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Authors
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P.M.Matias,
J.Tatur,
M.A.Carrondo,
W.R.Hagen.
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Ref.
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Acta Crystallogr Sect F Struct Biol Cryst Commun, 2005,
61,
503-506.
[DOI no: ]
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PubMed id
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Figure 1.
Crystals of P. furiosus ferritin. (a) 'As isolated',
[similar]17 Fe atoms per 24-mer. (b) Iron-containing ferritin,
[similar]1000 Fe atoms per 24-mer. The colour of the iron-loaded
protein solution and crystals prepared from it depends on the
amount of iron loaded and varies from light yellow to brown.
Acta Crystallogr Sect F Struct Biol Cryst Commun. 2005 May 1;
61(Pt 5): 503–506. Published online 2005 April 22. doi:
10.1107/S1744309105011516. Copyright [copyright] International
Union of Crystallography 2005
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Figure 2.
Self-rotation Patterson function plots for PfFtn in the
resolution range 3.5 [less-than-or-equal] d [less-than-or-equal]
15 A with integration range 5 [less-than-or-equal] R
[less-than-or-equal] 20 A. Peaks in the sections shown at
[kappa] = 90[deg] (a), [kappa] = 120[deg] (b) and [kappa] =
180[deg] (c) give the orientation of the crystallographic
twofold and non-crystallographic twofold, threefold and fourfold
(NCS) rotation axes in the crystal structure. The maximum value
was normalized to 100 and the contours drawn at five-unit
intervals, starting at 40. Drawings were prepared with programs
POLARRFN, NPO and XPLOT84DRIVER (Collaborative Computational
Project, Number 4, 1994[triangle]). Acta Crystallogr Sect F
Struct Biol Cryst Commun. 2005 May 1; 61(Pt 5): 503–506.
Published online 2005 April 22. doi: 10.1107/S1744309105011516.
Copyright [copyright] International Union of Crystallography
2005
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The above figures are
reproduced from the cited reference
which is an Open Access publication published by the IUCr
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