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      Construction of an enterobactin analogue with symmetrically arranged monomer subunits of ferritin

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          Abstract

          The symmetric arrangement of ferritin subunits served as a versatile foundation to produce a symmetric coordination space with designed ligands.

          Abstract

          A set of three catecholamide ligands mimicking the structure of enterobactin was constructed on ferritin, where the 3-fold symmetric arrangement of the monomer subunits served as a foundation to form a coordination space. Similar to enterobactin, the ligands showed strong affinity for the ferric ion and formed a tris-catechoyl complex. Crystallography revealed that the complex was embedded in the entrance of the 3-fold axis channel.

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          Ferritins: dynamic management of biological iron and oxygen chemistry.

          Xiaofeng Liu, Elizabeth C. Theil (2005)
          Ferritins are spherical, cage-like proteins with nanocavities formed by multiple polypeptide subunits (four-helix bundles) that manage iron/oxygen chemistry. Catalytic coupling yields diferric oxo/hydroxo complexes at ferroxidase sites in maxi-ferritin subunits (24 subunits, 480 kDa; plants, animals, microorganisms). Oxidation occurs at the cavity surface of mini-ferritins/Dps proteins (12 subunits, 240 kDa; bacteria). Oxidation products are concentrated as minerals in the nanocavity for iron-protein cofactor synthesis (maxi-ferritins) or DNA protection (mini-ferritins). The protein cage and nanocavity characterize all ferritins, although amino acid sequences diverge, especially in bacteria. Catalytic oxidation/di-iron coupling in the protein cage (maxi-ferritins, 480 kDa; plants, bacteria and animal cell-specific isoforms) or on the cavity surface (mini-ferritins/Dps proteins, 280 kDa; bacteria) initiates mineralization. Gated pores (eight or four), symmetrically arranged, control iron flow. The multiple ferritin functions combine pore, channel, and catalytic functions in compact protein structures required for life and disease response.
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            The ferritin superfamily: Supramolecular templates for materials synthesis.

            Masaki Uchida, Sebyung Kang, Courtney Reichhardt … (2010)
            Members of the ferritin superfamily are multi-subunit cage-like proteins with a hollow interior cavity. These proteins possess three distinct surfaces, i.e. interior and exterior surfaces of the cages and interface between subunits. The interior cavity provides a unique reaction environment in which the interior reaction is separated from the external environment. In biology the cavity is utilized for sequestration of irons and biomineralization as a mechanism to render Fe inert and sequester it from the external environment. Material scientists have been inspired by this system and exploited a range of ferritin superfamily proteins as supramolecular templates to encapsulate nanoparticles and/or as well-defined building blocks for fabrication of higher order assembly. Besides the interior cavity, the exterior surface of the protein cages can be modified without altering the interior characteristics. This allows us to deliver the protein cages to a targeted tissue in vivo or to achieve controlled assembly on a solid substrate to fabricate higher order structures. Furthermore, the interface between subunits is utilized for manipulating chimeric self-assembly of the protein cages and in the generation of symmetry-broken Janus particles. Utilizing these ideas, the ferritin superfamily has been exploited for development of a broad range of materials with applications from biomedicine to electronics. Copyright 2010 Elsevier B.V. All rights reserved.
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              Re-engineering protein interfaces yields copper-inducible ferritin cage assembly.

              Dustin J E Huard, Kathleen Kane, F. Akif Tezcan (2013)
              The ability to chemically control protein-protein interactions would allow the interrogation of dynamic cellular processes and lead to a better understanding and exploitation of self-assembling protein architectures. Here we introduce a new engineering strategy--reverse metal-templated interface redesign (rMeTIR)--that transforms a natural protein-protein interface into one that only engages in selective response to a metal ion. We have applied rMeTIR to render the self-assembly of the cage-like protein ferritin controllable by divalent copper binding, which has allowed the study of the structure and stability of the isolated ferritin monomer, the demonstration of the primary role of conserved hydrogen-bonding interactions in providing geometric specificity for cage assembly and the uniform chemical modification of the cage interior under physiological conditions. Notably, copper acts as a structural template for ferritin assembly in a manner that is highly reminiscent of RNA sequences that template virus capsid formation.
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                Author and article information

                Journal
                Journal ID (publisher-id): CHCOFS
                Title: Chemical Communications
                Abbreviated Title: Chem. Commun.
                Publisher: Royal Society of Chemistry (RSC)
                ISSN (Print): 1359-7345
                ISSN (Electronic): 1364-548X
                Publication date Created: 2015
                Publication date (Electronic): 2015
                Volume: 51
                Issue: 93
                Pages: 16609-16612
                Affiliations
                [1 ]Division of Molecular Materials Science
                [2 ]Graduate School of Science
                [3 ]Osaka City University
                [4 ]Osaka
                [5 ]Japan
                [6 ]Department of Chemistry
                [7 ]Nagoya University
                [8 ]Nagoya
                [9 ]Department of Biomolecular Engineering
                [10 ]Graduate School of Bioscience and Biotechnology
                [11 ]Tokyo Institute of Technology
                [12 ]Midori-ku
                [13 ]Research Centre of Materials Science
                Article
                DOI: 10.1039/C5CC06904A
                SO-VID: 23037659-d59b-4883-bc61-6663caded1dc
                Copyright © © 2015
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