5Z25

Trimeric Alpha-Helix-Inserted Circular Permutant of Cytochrome c555

5Z25 の概要

• エントリーDOI: 10.2210/pdb5z25/pdb
• 分子名称: Cytochrome c552, HEME C, TETRAETHYLENE GLYCOL, ... (4 entities in total)
• 機能のキーワード: permutant, electron transport
• 由来する生物種: Aquifex aeolicus (strain VF5); 詳細
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 11147.73

構造登録者

Oda, A.,Nagao, S.,Yamanaka, M.,Ueda, I.,Shibata, N.,Higuchi, Y.,Hirota, S. (登録日: 2017-12-28, 公開日: 2018-03-07, 最終更新日: 2024-10-30)

主引用文献

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

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: 29484831
DOI: 10.1002/asia.201800252

実験手法

X-RAY DIFFRACTION (1.7 Å)