2ZRQ
Crystal structure of S324A-subtilisin
2ZRQ の概要
| エントリーDOI | 10.2210/pdb2zrq/pdb |
| 関連するPDBエントリー | 2Z2X |
| 分子名称 | Tk-subtilisin, CALCIUM ION (3 entities in total) |
| 機能のキーワード | subtilisin, thermococcus kodakaraensis, calcium, hydrolase, protease, secreted, serine protease, zymogen |
| 由来する生物種 | Pyrococcus kodakaraensis (Thermococcus kodakaraensis) |
| 細胞内の位置 | Secreted: P58502 |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 34178.11 |
| 構造登録者 | Tanaka, S.,Takeuchi, Y.,Matsumura, H.,Koga, Y.,Takano, K.,Kanaya, S. (登録日: 2008-08-28, 公開日: 2009-03-03, 最終更新日: 2024-11-13) |
| 主引用文献 | Tanaka, S.,Takeuchi, Y.,Matsumura, H.,Koga, Y.,Takano, K.,Kanaya, S. Crystal structure of Tk-subtilisin folded without propeptide: requirement of propeptide for acceleration of folding Febs Lett., 582:3875-3878, 2008 Cited by PubMed Abstract: Tk-subtilisin (a subtilisin homologue from Thermococcus kodakaraensis) is matured from Pro-Tk-subtilisin upon autoprocessing and degradation of Tk-propeptide. To analyze the folding mechanism of Tk-subtilisin, the crystal structure of the active site mutant of Tk-subtilisin (S324A-subtilisin*), which was refolded in the presence of Ca2+ and absence of Tk-propeptide, was determined at 2.16A resolution. This structure is essentially the same as that of Tk-subtilisin matured from Pro-Tk-subtilisin. S324A-subtilisin* was refolded with a rate constant of 0.17 and 1.8min(-1) at 30 degrees C in the absence and presence of Tk-propeptide, respectively, indicating that Tk-subtilisin does not require Tk-propeptide for folding but requires it for acceleration of folding. PubMed: 18951896DOI: 10.1016/j.febslet.2008.10.025 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.16 Å) |
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