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Engineering protein assemblies with allosteric control via monomer fold-switching
dc.contributor.author | Campos, Luis | |
dc.contributor.author | Sadqi, Mourad | |
dc.contributor.author | Muñoz, Victor | |
dc.date.accessioned | 2020-01-08T13:54:11Z | |
dc.date.available | 2020-01-08T13:54:11Z | |
dc.date.issued | 2019 | |
dc.identifier.citation | 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. | es_ES |
dc.identifier.uri | http://hdl.handle.net/10481/58553 | |
dc.description.abstract | 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. | es_ES |
dc.description.sponsorship | This work was supported by the European Research Council (grant ERC-2012-ADG- 323059 to V.M.) and by the PRODESTECH network funded through the CONSOLIDER program from the Spanish Government (grant CSD2009-00088). L.A.C. acknowledges support from Ministry of Economy and Competitiveness through grants BIO2016- 78768-P and RYC-2013-13197. V.M. acknowledges additional support from the W.M. Keck Foundation and from the CREST Center for Cellular and Biomomolecular Machines (grant NSF-CREST-1547848). J.M.V. acknowledges additional support from Ministry of Economy and Competitiveness through grant BFU2016-75984. F.M.R. and A.R. thank the staff from the ALBA synchrotron (Spain) for assistance with the XALOC beamline. Structural data are deposited in the Protein Data Bank with accession codes 6QIY (X-ray CI2 classical geometry) and 6QIZ (X-ray CI2 domain swapped) and EMD- 4568 (cryo-EM CI2eng assembly). | es_ES |
dc.language.iso | eng | es_ES |
dc.publisher | Springer Nature | es_ES |
dc.rights | Atribución 3.0 España | * |
dc.rights.uri | http://creativecommons.org/licenses/by/3.0/es/ | * |
dc.title | Engineering protein assemblies with allosteric control via monomer fold-switching | es_ES |
dc.type | info:eu-repo/semantics/article | es_ES |
dc.rights.accessRights | info:eu-repo/semantics/openAccess | es_ES |
dc.identifier.doi | 10.1038/s41467-019-13686-1 |