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Crystal Structures of a Tetrahedral Open Pore Ferritin from the Hyperthermophilic Archaeon Archaeoglobus fulgidus

Eric E Johnson, Duilio D Cascio, Michael R MR Sawaya, Mari M Gingery, and Imke I Schröder

Structure 13(4):12 (2005) PMID 15837202

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 (~45 A) pores in the AfFtn shell. Two nonconservative amino acid substitutions may be critical for stabilizing the tetrahedral form.

Copyright © 2005 Elsevier Ltd. All rights reserved.

DOI: 10.1016/j.str.2005.01.019
Version: za2963e q8zab q8zbd q8zc9 q8zd7 q8zeb q8zfd q8zgc

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