2ZRQ
Crystal structure of S324A-subtilisin
Summary for 2ZRQ
| Entry DOI | 10.2210/pdb2zrq/pdb |
| Related | 2Z2X |
| Descriptor | Tk-subtilisin, CALCIUM ION (3 entities in total) |
| Functional Keywords | subtilisin, thermococcus kodakaraensis, calcium, hydrolase, protease, secreted, serine protease, zymogen |
| Biological source | Pyrococcus kodakaraensis (Thermococcus kodakaraensis) |
| Cellular location | Secreted: P58502 |
| Total number of polymer chains | 1 |
| Total formula weight | 34178.11 |
| Authors | Tanaka, S.,Takeuchi, Y.,Matsumura, H.,Koga, Y.,Takano, K.,Kanaya, S. (deposition date: 2008-08-28, release date: 2009-03-03, Last modification date: 2024-11-13) |
| Primary citation | 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 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.16 Å) |
Structure validation
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