Archaeal Lsm rings as stable self-assembling tectons for protein nanofabrication

We have exploited the self-assembling properties of archaeal-derived protein Lsmα to generate new supramolecular forms based on its stable ring-shaped heptamer. We show that engineered ring tectons incorporating cysteine sidechains on obverse faces of the Lsmα7 toroid are capable of forming paired and stacked formations. A Cys-modified construct, N10C/E61C-Lsmα, appears to organize into disulfide-mediated tube formations up to 45 nm in length. We additionally report fabrication of cage-like protein clusters through conjugation of Cu2+ to His-tagged variants of the Lsmα7 tecton. These 400 kDa protein capsules are seen as cube particles with visible pores, and are reversibly dissembled into their component ring tectons by EDTA. The β-rich Lsmα supramolecular assemblies described are amenable to further fusion modifications, or for surface attachment, so providing potential for future applications that exploit the RNA-binding capacity of Lsm proteins, such as sensing applications. [Display omitted] •Archaeal Lsmα protein self-assembles in vitro into a stable heptameric ring with 1.5 nm pore.•Cys modification at ring surfaces covalently links [Lsmα]7 into pair and tube-like conjugations.•When exposed to Cu2+, His-tagged variants form discrete cage-like nanostructures.•[Lsmα]7 provides a new ring tecton for protein-based porous materials.