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TitleEngineering protein assemblies with allosteric control via monomer fold-switching.
Journal, issue, pagesNat Commun, Vol. 10, Issue 1, Page 5703, Year 2019
Publish dateDec 13, 2019
AuthorsLuis 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 AbstractThe 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.
External linksNat Commun / PubMed:31836707 / PubMed Central
MethodsEM (single particle) / X-ray diffraction
Resolution1.5 - 8.55 Å
Structure data

EMDB-4568:
Cryo-EM 3D structure of CI2eng toroidal dodecameric assembly.
Method: EM (single particle) / Resolution: 8.55 Å

PDB-6qiy:
CI-2, conformation 1
Method: X-RAY DIFFRACTION / Resolution: 1.5 Å

PDB-6qiz:
CI-2, conformation 2
Method: X-RAY DIFFRACTION / Resolution: 1.65 Å

Chemicals

ChemComp-HOH:
WATER

Source
  • hordeum vulgare (barley)
KeywordsPLANT PROTEIN / CHYMOTRYPSIN INHIBITOR 2 / protease inhibitor / hydrolase inhibitor

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