5Z25
Trimeric Alpha-Helix-Inserted Circular Permutant of Cytochrome c555
Summary for 5Z25
| Entry DOI | 10.2210/pdb5z25/pdb |
| Descriptor | Cytochrome c552, HEME C, TETRAETHYLENE GLYCOL, ... (4 entities in total) |
| Functional Keywords | permutant, electron transport |
| Biological source | Aquifex aeolicus (strain VF5) More |
| Total number of polymer chains | 1 |
| Total formula weight | 11147.73 |
| Authors | Oda, A.,Nagao, S.,Yamanaka, M.,Ueda, I.,Shibata, N.,Higuchi, Y.,Hirota, S. (deposition date: 2017-12-28, release date: 2018-03-07, Last modification date: 2024-10-30) |
| Primary citation | Oda, A.,Nagao, S.,Yamanaka, M.,Ueda, I.,Watanabe, H.,Uchihashi, T.,Shibata, N.,Higuchi, Y.,Hirota, S. Construction of a Triangle-Shaped Trimer and a Tetrahedron Using an alpha-Helix-Inserted Circular Permutant of Cytochrome c555. Chem Asian J, 13:964-967, 2018 Cited by 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 , 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 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. PubMed: 29484831DOI: 10.1002/asia.201800252 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.7 Å) |
Structure validation
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