2DF5
Crystal Structure of Pf-PCP(1-204)-C
2DF5 の概要
| エントリーDOI | 10.2210/pdb2df5/pdb |
| 関連するPDBエントリー | 1IOF |
| 分子名称 | Pyrrolidone-carboxylate peptidase (2 entities in total) |
| 機能のキーワード | chameleon sequence, pyrococcus furiosus, pyrrolidone carboxyl peptidase, hydrolase |
| 由来する生物種 | Pyrococcus furiosus |
| 細胞内の位置 | Cytoplasm: O73944 |
| タンパク質・核酸の鎖数 | 4 |
| 化学式量合計 | 93549.52 |
| 構造登録者 | Katagiri, Y.,Takano, K.,Chon, H.,Matsumura, H.,Koga, Y.,Kanaya, S. (登録日: 2006-02-24, 公開日: 2007-03-06, 最終更新日: 2023-10-25) |
| 主引用文献 | Takano, K.,Katagiri, Y.,Mukaiyama, A.,Chon, H.,Matsumura, H.,Koga, Y.,Kanaya, S. Conformational contagion in a protein: structural properties of a chameleon sequence Proteins, 68:617-625, 2007 Cited by PubMed Abstract: Certain sequences, known as chameleon sequences, take both alpha- and beta-conformations in natural proteins. We demonstrate that a wild chameleon sequence fused to the C-terminal alpha-helix or beta-sheet in foreign stable proteins from hyperthermophiles forms the same conformation as the host secondary structure. However, no secondary structural formation is observed when the sequence is attached to the outside of the secondary structure. These results indicate that this sequence inherently possesses an ability to make either alpha- or beta-conformation, depending on the sequentially neighboring secondary structure if little other nonlocal interaction occurs. Thus, chameleon sequences take on a satellite state through contagion by the power of a secondary structure. We propose this "conformational contagion" as a new nonlocal determinant factor in protein structure and misfolding related to protein conformational diseases. PubMed: 17510955DOI: 10.1002/prot.21451 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.3 Å) |
構造検証レポート
検証レポート(詳細版)
をダウンロード






