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. 2014 May 19;111(22):7925–7930. doi: 10.1073/pnas.1318417111

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Fig. 1. — Ion channels in soluble ferritin protein nanocages transport Fe²⁺ to multiple catalytic centers (F_ox or oxidoreductase sites). (A) The 24-subunit ferritin protein cage. Red helices, Fe²⁺ channels. (B) A ferritin Fe²⁺ ion channel (side view). Green spheres, metal ions. Conserved residues E57 and E136 are putative carboxylate links in Fe²⁺ transit between ferritin ion channel carboxylate (E130 and D127) and ferritin enzyme (F_ox) sites based on phylogenetic structural location and conformational flexibility in protein crystals (16, 18). (C) A single ferritin protein cage subunit (side view). Tan, channel helix segments. (D) Ion channel (viewed from inside the protein cage). Green spheres, metal ions. Prepared from PDB 3KA3 using PyMol.