Unknown

Dataset Information

0

Metal-Templated Design of Chemically Switchable Protein Assemblies with High-Affinity Coordination Sites.


ABSTRACT: To mimic a hypothetical pathway for protein evolution, we previously tailored a monomeric protein (cyt cb562 ) for metal-mediated self-assembly, followed by re-design of the resulting oligomers for enhanced stability and metal-based functions. We show that a single hydrophobic mutation on the cyt cb562 surface drastically alters the outcome of metal-directed oligomerization to yield a new trimeric architecture, (TriCyt1)3. This nascent trimer was redesigned into second and third-generation variants (TriCyt2)3 and (TriCyt3)3 with increased structural stability and preorganization for metal coordination. The three TriCyt variants combined furnish a unique platform to 1) provide tunable coupling between protein quaternary structure and metal coordination, 2) enable the construction of metal/pH-switchable protein oligomerization motifs, and 3) generate a robust metal coordination site that can coordinate all mid-to-late first-row transition-metal ions with high affinity.

SUBMITTER: Kakkis A 

PROVIDER: S-EPMC7983065 | biostudies-literature |

REPOSITORIES: biostudies-literature

Similar Datasets

| S-EPMC11338832 | biostudies-literature
| S-EPMC2836610 | biostudies-literature
| S-EPMC6432594 | biostudies-literature
| S-EPMC6115636 | biostudies-literature
| S-EPMC5131729 | biostudies-literature
| S-EPMC2613763 | biostudies-literature
| S-EPMC6802106 | biostudies-literature
| S-EPMC8317668 | biostudies-literature
| S-EPMC7429910 | biostudies-literature
| S-EPMC9299919 | biostudies-literature