ChemBioChem
ChemBioChem
5 years ago

Symmetry-Directed Self-Assembly of a Tetrahedral Protein Cage Mediated by de Novo-Designed Coiled Coils

Symmetry-Directed Self-Assembly of a Tetrahedral Protein Cage Mediated by de Novo-Designed Coiled Coils
James C. A. Bardwell, Aaron Sciore, Ajitha S. Cristie-David, Philipp Koldewey, Joseph D. Eschweiler, Somayesadat Badieyan, E. Neil G. Marsh, Brandon T. Ruotolo, Min Su
The cover picture shows the application of symmetry principles to assembling proteins into geometrical cages. In their communication, E. N. G. Marsh et al. explain how they used a small, trimeric, coiled-coil domain to assemble a trimeric enzyme into a well-defined tetrahedral cage. This was achieved by genetically fusing the coiled-coil domain to the C terminus of the enzyme protein through a flexible polyglycine linker sequence—the coiled-coil acts as a molecular “twist-tie” to hold the cage together. Other than optimizing the strength of the coiled-coil interaction and the length of the glycine linker, no further constraints were needed to assemble the desired tetrahedral cage in high yield. This methodology provides a flexible and modular symmetry-based approach to assembling polyhedral protein cages that can be expanded to use de novo-designed coiled coils as off-the-shelf components for protein assembly.

Publisher URL: http://onlinelibrary.wiley.com/resolve/doi

DOI: 10.1002/cbic.201700481

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