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PDBsum entry 7jgo
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Oxidoreductase
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PDB id
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7jgo
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References listed in PDB file
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Key reference
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Title
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Tunable and cooperative thermomechanical properties of protein-Metal-Organic frameworks.
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Authors
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J.B.Bailey,
F.A.Tezcan.
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Ref.
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J Am Chem Soc, 2020,
142,
17265-17270.
[DOI no: ]
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PubMed id
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Abstract
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We recently introduced protein-metal-organic frameworks (protein-MOFs) as
chemically designed protein crystals, composed of ferritin nodes that
predictably assemble into 3D lattices upon coordination of various metal ions
and ditopic, hydroxamate-based linkers. Owing to their unique tripartite
construction, protein-MOFs possess extremely sparse lattice connectivity,
suggesting that they might display unusual thermomechanical properties.
Leveraging the synthetic modularity of ferritin-MOFs, we investigated the
temperature-dependent structural dynamics of six distinct frameworks. Our
results show that the thermostabilities of ferritin-MOFs can be tuned through
the metal component or the presence of crowding agents. Our studies also reveal
a framework that undergoes a reversible and isotropic first-order phase
transition near-room temperature, corresponding to a 4% volumetric change within
1 °C and a hysteresis window of ∼10 °C. This highly cooperative
crystal-to-crystal transformation, which stems from the soft crystallinity of
ferritin-MOFs, illustrates the advantage of modular construction strategies in
discovering tunable-and unpredictable-material properties.
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