Construction of a Triangle-Shaped Trimer and a Tetrahedron Using an α-Helix-Inserted Circular Permutant of Cytochrome c555

Chemistry, an Asian Journal
Akiya OdaShun Hirota

Abstract

Highly-ordered protein structures have gained interest for future uses for biomaterials. Herein, we constructed a building block protein (BBP) by the circular permutation of the hyperthermostable Aquifex aeolicus cytochrome (cyt) c555 , and assembled BBP into a triangle-shaped trimer and a tetrahedron. The angle of the intermolecular interactions of BBP was controlled by cleaving the domain-swapping hinge loop of cyt c555 and connecting the original N- and C-terminal α-helices with an α-helical linker. We obtained BBP oligomers up to ≈40 mers, with a relatively large amount of trimers. According to the X-ray crystallographic analysis of the BBP trimer, the N-terminal region of one BBP molecule interacted intermolecularly with the C-terminal region of another BBP molecule, resulting in a triangle-shaped structure with an edge length of 68 Å. Additionally, four trimers assembled into a unique tetrahedron in the crystal. These results demonstrate that the circular permutation connecting the original N- and C-terminal α-helices with an α-helical linker may be useful for constructing organized protein structures.

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Citations

Jan 21, 2020·Metallomics : Integrated Biometal Science·Robby Noor CahyonoShun Hirota
Aug 23, 2019·Biochimica Et Biophysica Acta. Proteins and Proteomics·Hongxu YangShun Hirota
Feb 13, 2021·Journal of Inorganic Biochemistry·Satoshi NagaoShun Hirota
Oct 30, 2021·Chemical Communications : Chem Comm·Shun HirotaNaoya Kobayashi

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