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| Title | Self-assembly and regulation of protein cages from pre-organised coiled-coil modules. |
|---|---|
| Journal, issue, pages | Nat Commun, Vol. 12, Issue 1, Page 939, Year 2021 |
| Publish date | Feb 11, 2021 |
 Authors | Fabio Lapenta / Jana Aupič / Marco Vezzoli / Žiga Strmšek / Stefano Da Vela / Dmitri I Svergun / José María Carazo / Roberto Melero / Roman Jerala /     |
| PubMed Abstract | Coiled-coil protein origami (CCPO) is a modular strategy for the de novo design of polypeptide nanostructures. CCPO folds are defined by the sequential order of concatenated orthogonal coiled-coil ...Coiled-coil protein origami (CCPO) is a modular strategy for the de novo design of polypeptide nanostructures. CCPO folds are defined by the sequential order of concatenated orthogonal coiled-coil (CC) dimer-forming peptides, where a single-chain protein is programmed to fold into a polyhedral cage. Self-assembly of CC-based nanostructures from several chains, similarly as in DNA nanotechnology, could facilitate the design of more complex assemblies and the introduction of functionalities. Here, we show the design of a de novo triangular bipyramid fold comprising 18 CC-forming segments and define the strategy for the two-chain self-assembly of the bipyramidal cage from asymmetric and pseudo-symmetric pre-organised structural modules. In addition, by introducing a protease cleavage site and masking the interfacial CC-forming segments in the two-chain bipyramidal cage, we devise a proteolysis-mediated conformational switch. This strategy could be extended to other modular protein folds, facilitating the construction of dynamic multi-chain CC-based complexes. |
 External links | Nat Commun / PubMed:33574245 / PubMed Central |
| Methods | EM (single particle) |
| Resolution | 25.0 Å |
| Structure data |  EMDB-11831: |
| Source |
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Escherichia coli (E. coli)