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Symmetry‐Directed Self‐Assembly of a Tetrahedral Protein Cage Mediated by de Novo‐Designed Coiled Coils
Author(s) -
Badieyan Somayesadat,
Sciore Aaron,
Eschweiler Joseph D.,
Koldewey Philipp,
CristieDavid Ajitha S.,
Ruotolo Brandon T.,
Bardwell James C. A.,
Su Min,
Marsh E. Neil G.
Publication year - 2017
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.201700406
Subject(s) - linker , coiled coil , tetrahedron , protein engineering , cage , protein design , symmetry (geometry) , self assembly , translational symmetry , protein structure , sequence (biology) , domain (mathematical analysis) , crystallography , nanotechnology , chemistry , biophysics , materials science , biology , computer science , biochemistry , physics , enzyme , combinatorics , mathematics , geometry , mathematical analysis , condensed matter physics , operating system
The organization of proteins into new hierarchical forms is an important challenge in synthetic biology. However, engineering new interactions between protein subunits is technically challenging and typically requires extensive redesign of protein–protein interfaces. We have developed a conceptually simple approach, based on symmetry principles, that uses short coiled‐coil domains to assemble proteins into higher‐order structures. Here, we demonstrate the assembly of a trimeric enzyme into a well‐defined tetrahedral cage. This was achieved by genetically fusing a trimeric coiled‐coil domain to its C terminus through a flexible polyglycine linker sequence. The linker length and coiled‐coil strength were the only parameters that needed to be optimized to obtain a high yield of correctly assembled protein cages.