Structural highlights
FunctionPublication Abstract from PubMedHighly-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 tetrahedral structure. 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 alpha-helices with an alpha-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 A. Additionally, four trimers assembled into a unique tetrahedral structure in the crystal. These results demonstrate that the circular permutation connecting the original N- and C-terminal alpha-helices with an alpha-helical linker may be useful for constructing organized protein structures. Construction of a Triangle-Shaped Trimer and a Tetrahedral Structure Using an alpha-Helix-Inserted Circular Permutant of Cytochrome c(5)(5)(5).,Oda A, Nagao S, Yamanaka M, Ueda I, Watanabe H, Uchihashi T, Shibata N, Higuchi Y, Hirota S Chem Asian J. 2018 Feb 26. doi: 10.1002/asia.201800252. PMID:29484831[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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