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Título: | Engineering protein assemblies with allosteric control via monomer fold-switching |
Autor: | Campos, Luis A. CSIC ORCID; Sharma, Rajendra; Alvira, Sara; Ruiz, Federico M. CSIC ORCID ; Ibarra-Molero, Beatriz; Sadqi, Mourad CSIC ORCID; Alfonso, Carlos CSIC ORCID ; Rivas, Germán CSIC ORCID CVN ; Sánchez-Ruiz, Jose M.; Romero, Antonio CSIC ORCID ; Valpuesta, José M. CSIC ORCID ; Muñoz, Víctor CSIC ORCID | Fecha de publicación: | 13-dic-2019 | Editor: | Nature Publishing Group | Citación: | Nature Communications | Resumen: | The macromolecular machines of life use allosteric control to self-assemble, dissociate and change shape in response to signals. Despite enormous interest, the design of nanoscale allosteric assemblies has proven tremendously challenging. Here we present a proof of concept of allosteric assembly in which an engineered fold switch on the protein monomer triggers or blocks assembly. Our design is based on the hyper-stable, naturally monomeric protein CI2, a paradigm of simple two-state folding, and the toroidal arrangement with 6-fold symmetry that it only adopts in crystalline form. We engineer CI2 to enable a switch between the native and an alternate, latent fold that self-assembles onto hexagonal toroidal particles by exposing a favorable inter-monomer interface. The assembly is controlled on demand via the competing effects of temperature and a designed short peptide. These findings unveil a remarkable potential for structural metamorphosis in proteins and demonstrate key principles for engineering protein-based nanomachinery. | URI: | http://hdl.handle.net/10261/219612 | ISSN: | 2041-1723 |
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