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. 2020 Apr 17;37(9):2711–2726. doi: 10.1093/molbev/msaa100

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© The Author(s) 2020. Published by Oxford University Press on behalf of the Society for Molecular Biology and Evolution.

This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted reuse, distribution, and reproduction in any medium, provided the original work is properly cited.

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Fig. 9. — The conserved structural core of proteins in the ferritin-like superfamily comprises a four-helix bundle that coordinates a pair of metal ions. The helices are arranged in a characteristic up-down–down-up topology. Shown here are representative structures from the ferritin (2za7A), bacterioferritin (1nfvA), and Dps (1o9rA) groups colored from (red) N-terminus to (blue) C-terminus (a) ferritin, (b) bacterioferritin, (c) Dps, (d) overlaid (ferritin, red; bacterioferritin, green; Dps, blue).