The symmetric designer protein Pizza as a scaffold for metal coordination

Abstract Symmetric proteins are currently of interest as they allow creation larger assemblies and facilitate the incorporation metal ions in complexes. Recently this was demonstrated by biomineralization cadmium‐chloride nanocrystal via Pizza designer protein. However, mechanism behind formation remained unclear. Here, we set out to investigate driving truncation, mutation, circular permutations. In addition, interaction other biologically relevant with these symmetric form complexes also studied. The initial is shown originate from steric strain, where His 58 induces a different rotameric conformation on 73, thereby distorting an otherwise perfect planar ring alternating cadmium chlorine ions, resulting smallest nanocrystal. Similar highly were observed for biological ions. flexibility coordinating histidine residues allows each ion adopt its preferred geometry leading either monomeric or dimeric β ‐propeller units, located at interface between both propeller units. These results demonstrate that not only interesting generate assemblies, but scaffold create more complex based assemblies. Such protein may then find applications bionanotechnology biocatalysis.