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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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References listed in PDB file
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Key reference
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Title
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Crystal structures of a tetrahedral open pore ferritin from the hyperthermophilic archaeon archaeoglobus fulgidus.
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Authors
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E.Johnson,
D.Cascio,
M.R.Sawaya,
M.Gingery,
I.Schröder.
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Ref.
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Structure, 2005,
13,
637-648.
[DOI no: ]
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PubMed id
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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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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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