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-Structure paper
タイトル | Engineering protein assemblies with allosteric control via monomer fold-switching. |
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ジャーナル・号・ページ | Nat Commun, Vol. 10, Issue 1, Page 5703, Year 2019 |
掲載日 | 2019年12月13日 |
著者 | Luis A Campos / Rajendra Sharma / Sara Alvira / Federico M Ruiz / Beatriz Ibarra-Molero / Mourad Sadqi / Carlos Alfonso / Germán Rivas / Jose M Sanchez-Ruiz / Antonio Romero Garrido / José M Valpuesta / Victor Muñoz / |
PubMed 要旨 | 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 ...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. |
リンク | Nat Commun / PubMed:31836707 / PubMed Central |
手法 | EM (単粒子) / X線回折 |
解像度 | 1.5 - 8.55 Å |
構造データ | EMDB-4568: PDB-6qiy: PDB-6qiz: |
化合物 | ChemComp-HOH: |
由来 |
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キーワード | PLANT PROTEIN (植物) / CHYMOTRYPSIN INHIBITOR 2 / protease inhibitor (プロテアーゼ阻害剤) / hydrolase inhibitor |