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• W2955117988 endingPage "1629" @default.
• W2955117988 startingPage "1620" @default.
• W2955117988 abstract "Short, alpha-helical coiled coils provide a simple, modular method to direct the assembly of proteins into higher order structures. We previously demonstrated that by genetically fusing de novo–designed coiled coils of the appropriate oligomerization state to a natural trimeric protein, we could direct the assembly of this protein into various geometrical cages. Here, we have extended this approach by appending a coiled coil designed to trimerize in response to binding divalent transition metal ions and thereby achieve metal ion-dependent assembly of a tetrahedral protein cage. Ni2+, Co2+, Cu2+, and Zn2+ ions were evaluated, with Ni2+ proving the most effective at mediating protein assembly. Characterization of the assembled protein indicated that the metal ion–protein complex formed discrete globular structures of the diameter expected for a complex containing 12 copies of the protein monomer. Protein assembly could be reversed by removing metal ions with ethylenediaminetetraacetic acid or under mildly acidic conditions." @default.
• W2955117988 created "2019-07-12" @default.
• W2955117988 creator A5057584218 @default.
• W2955117988 creator A5088885688 @default.
• W2955117988 date "2019-08-06" @default.
• W2955117988 modified "2023-10-01" @default.
• W2955117988 title "Metal‐dependent assembly of a protein nano‐cage" @default.
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• W2955117988 doi "https://doi.org/10.1002/pro.3676" @default.
• W2955117988 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/6699099" @default.
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• W2955117988 hasPublicationYear "2019" @default.
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