Download MendeleyConstruction of a Triangle-Shaped Trimer and a Tetrahedron Using an alpha-Helix-Inserted Circular Permutant of Cytochrome c555.
Oda, A., Nagao, S., Yamanaka, M., Ueda, I., Watanabe, H., Uchihashi, T., Shibata, N., Higuchi, Y., Hirota, S.(2018) Chem Asian J 13: 964-967
- PubMed: 29484831
- DOI: https://doi.org/10.1002/asia.201800252
- Primary Citation of Related Structures:
5Z25 - PubMed 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) c 555 , 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 c 555 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.
Organizational Affiliation:
Graduate School of Materials Science, Nara Institute of Science and Technology, 8916-5 Takayama, Ikoma, Nara, 630-0192, Japan.
