1S3Q

Crystal structures of a novel open pore ferritin from the hyperthermophilic Archaeon Archaeoglobus fulgidus

Summary for 1S3Q

• Entry DOI: 10.2210/pdb1s3q/pdb
• Descriptor: ferritin, ZINC ION (3 entities in total)
• Functional Keywords: ferroxidase, four helix bundle, iron storage, metal binding protein
• Biological source: Archaeoglobus fulgidus
• Total number of polymer chains: 12
• Total formula weight: 250691.48

Authors

Johnson, E.,Cascio, D.,Sawaya, M.,Schroeder, I. (deposition date: 2004-01-13, release date: 2005-04-12, Last modification date: 2024-11-13)

Primary citation

Johnson, E.,Cascio, D.,Sawaya, M.R.,Gingery, M.,Schroder, I.
Crystal structures of a tetrahedral open pore ferritin from the hyperthermophilic archaeon Archaeoglobus fulgidus.
Structure, 13:637-648, 2005

PubMed Abstract: 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.

PubMed: 15837202
DOI: 10.1016/j.str.2005.01.019

Experimental method

X-RAY DIFFRACTION (2.1 Å)