1sq3
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Crystal structures of a novel open pore ferritin from the hyperthermophilic Archaeon Archaeoglobus fulgidus.
OverviewOverview
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.
About this StructureAbout this Structure
1SQ3 is a Single protein structure of sequence from Archaeoglobus fulgidus dsm 4304 with FE as ligand. Full crystallographic information is available from OCA.
ReferenceReference
Crystal structures of a tetrahedral open pore ferritin from the hyperthermophilic archaeon Archaeoglobus fulgidus., Johnson E, Cascio D, Sawaya MR, Gingery M, Schroder I, Structure. 2005 Apr;13(4):637-48. PMID:15837202
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