Engineering protein assemblies with allosteric control via monomer fold-switching Campos, Luis Sadqi, Mourad Muñoz, Victor 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. 2020-01-08T13:54:11Z 2020-01-08T13:54:11Z 2019 journal article Campos, L. A., Sharma, R., Alvira, S., Ruiz, F. M., Ibarra-Molero, B., Sadqi, M., ... & Valpuesta, J. M. (2019). Engineering protein assemblies with allosteric control via monomer fold-switching. Nature Communications, 10(1), 1-13. http://hdl.handle.net/10481/58553 10.1038/s41467-019-13686-1 eng http://creativecommons.org/licenses/by/3.0/es/ open access Atribución 3.0 España Springer Nature