Unknown

Dataset Information

0

Metal-dependent assembly of a protein nano-cage.


ABSTRACT: Short, alpha-helical coiled coils provide a simple, modular method to direct the assembly of proteins into higher order structures. We previously demonstrated that by genetically fusing de novo-designed coiled coils of the appropriate oligomerization state to a natural trimeric protein, we could direct the assembly of this protein into various geometrical cages. Here, we have extended this approach by appending a coiled coil designed to trimerize in response to binding divalent transition metal ions and thereby achieve metal ion-dependent assembly of a tetrahedral protein cage. Ni2+ , Co2+ , Cu2+ , and Zn2+ ions were evaluated, with Ni2+ proving the most effective at mediating protein assembly. Characterization of the assembled protein indicated that the metal ion-protein complex formed discrete globular structures of the diameter expected for a complex containing 12 copies of the protein monomer. Protein assembly could be reversed by removing metal ions with ethylenediaminetetraacetic acid or under mildly acidic conditions.

SUBMITTER: Cristie-David AS 

PROVIDER: S-EPMC6699099 | biostudies-literature | 2019 Sep

REPOSITORIES: biostudies-literature

altmetric image

Publications

Metal-dependent assembly of a protein nano-cage.

Cristie-David Ajitha S AS   Marsh E Neil G ENG  

Protein science : a publication of the Protein Society 20190806 9


Short, alpha-helical coiled coils provide a simple, modular method to direct the assembly of proteins into higher order structures. We previously demonstrated that by genetically fusing de novo-designed coiled coils of the appropriate oligomerization state to a natural trimeric protein, we could direct the assembly of this protein into various geometrical cages. Here, we have extended this approach by appending a coiled coil designed to trimerize in response to binding divalent transition metal  ...[more]

Similar Datasets

| S-EPMC2275108 | biostudies-other
| S-EPMC6729141 | biostudies-literature
| S-EPMC8185198 | biostudies-literature
| S-EPMC2852946 | biostudies-literature
| S-EPMC5870838 | biostudies-literature
| S-EPMC8730398 | biostudies-literature
| S-EPMC9854185 | biostudies-literature
| S-EPMC5241807 | biostudies-other
| S-EPMC6354838 | biostudies-literature
| S-EPMC8153215 | biostudies-literature