1PMA
PROTEASOME FROM THERMOPLASMA ACIDOPHILUM
1PMA の概要
| エントリーDOI | 10.2210/pdb1pma/pdb |
| 分子名称 | PROTEASOME (2 entities in total) |
| 機能のキーワード | protease, proteasome, hydrolase |
| 由来する生物種 | Thermoplasma acidophilum 詳細 |
| 細胞内の位置 | Cytoplasm (By similarity): P25156 P28061 |
| タンパク質・核酸の鎖数 | 28 |
| 化学式量合計 | 685989.61 |
| 構造登録者 | Loewe, J.,Stock, D.,Jap, B.,Zwickl, P.,Baumeister, W.,Huber, R. (登録日: 1994-12-19, 公開日: 1996-06-20, 最終更新日: 2024-02-14) |
| 主引用文献 | Lowe, J.,Stock, D.,Jap, B.,Zwickl, P.,Baumeister, W.,Huber, R. Crystal structure of the 20S proteasome from the archaeon T. acidophilum at 3.4 A resolution. Science, 268:533-539, 1995 Cited by PubMed Abstract: The three-dimensional structure of the proteasome from the archaebacterium Thermoplasma acidophilum has been elucidated by x-ray crystallographic analysis by means of isomorphous replacement and cyclic averaging. The atomic model was built and refined to a crystallographic R factor of 22.1 percent. The 673-kilodalton protease complex consists of 14 copies of two different subunits, alpha and beta, forming a barrel-shaped structure of four stacked rings. The two inner rings consist of seven beta subunits each, and the two outer rings consist of seven alpha subunits each. A narrow channel controls access to the three inner compartments. The alpha 7 beta 7 beta 7 alpha 7 subunit assembly has 72-point group symmetry. The structures of the alpha and beta subunits are similar, consisting of a core of two antiparallel beta sheets that is flanked by alpha helices on both sides. The binding of a peptide aldehyde inhibitor marks the active site in the central cavity at the amino termini of the beta subunits and suggests a novel proteolytic mechanism. PubMed: 7725097主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (3.4 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






