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The symmetric designer protein Pizza as a scaffold for metal coordination

DOI: 10.1002/prot.26072 DOI Help

Authors: Jeroen P. M. Vrancken (KU Leuven) , Hiroki Noguchi (KU Leuven) , Kam Y. J. Zhang (RIKEN) , Jeremy R. H. Tame (Yokohama City University) , Arnout R. D. Voet (KU Leuven)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Proteins: Structure, Function, And Bioinformatics , VOL 134

State: Published (Approved)
Published: March 2021
Diamond Proposal Number(s): 19190 , 17167

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

Journal Keywords: biotechnology; metalloprotein; protein design; structural biology

Subject Areas: Biology and Bio-materials, Chemistry

Instruments: I04-Macromolecular Crystallography

Other Facilities: 5.2R beamline at Elettra; 17A at Photon Factory; BL41XU beamline at SPring8; Proxima‐1 at SOLEIL; PX‐III at Swiss Light Source

Added On: 19/04/2021 14:27

Discipline Tags:

Physical Chemistry Biochemistry Catalysis Chemistry Structural biology Life Sciences & Biotech

Technical Tags:

Diffraction Macromolecular Crystallography (MX)