Elaborating a coiled‐coil‐assembled octahedral protein cage with additional protein domains
| Autor: | Philipp Koldewey, Ajitha S. Cristie-David, Ben A. Meinen, James C.A. Bardwell, E. Neil G. Marsh |
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| Rok vydání: | 2018 |
| Předmět: |
Models
Molecular 0301 basic medicine Protein Folding Full‐Length Papers Physics::Medical Physics Protein design Protein domain Biochemistry Maltose-Binding Proteins Quantitative Biology::Subcellular Processes 03 medical and health sciences Maltose-binding protein Synthetic biology Protein Domains Escherichia coli Physics::Atomic and Molecular Clusters Amino Acid Sequence Amino Acids Molecular Biology Coiled coil Quantitative Biology::Biomolecules biology Chemistry Quantitative Biology::Molecular Networks Molecular Weight Crystallography Cross-Linking Reagents 030104 developmental biology Octahedron biology.protein Tetrahedron Protein Multimerization Cage |
| Zdroj: | Protein Science. 27:1893-1900 |
| ISSN: | 1469-896X 0961-8368 |
| DOI: | 10.1002/pro.3497 |
| Popis: | De novo design of protein nano‐cages has potential applications in medicine, synthetic biology, and materials science. We recently developed a modular, symmetry‐based strategy for protein assembly in which short, coiled‐coil sequences mediate the assembly of a protein building block into a cage. The geometry of the cage is specified by the combination of rotational symmetries associated with the coiled‐coil and protein building block. We have used this approach to design well‐defined octahedral and tetrahedral cages. Here, we show that the cages can be further elaborated and functionalized by the addition of another protein domain to the free end of the coiled‐coil: in this case by fusing maltose‐binding protein to an octahedral protein cage to produce a structure with a designed molecular weight of ~1.8 MDa. Importantly, the addition of the maltose binding protein domain dramatically improved the efficiency of assembly, resulting in ~ 60‐fold greater yield of purified protein compared to the original cage design. This study shows the potential of using small, coiled‐coil motifs as off‐the‐shelf components to design MDa‐sized protein cages to which additional structural or functional elements can be added in a modular manner. |
| Databáze: | OpenAIRE |
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