EC Number   |
Reference |
|---|
   3.4.21.B57 | crystallization of the active-site mutant S255A of pro-Tk-subtilisin. The crystal is grown at 4°C by the sitting-drop vapour-diffusion method. Native X-ray diffraction data are collected to 2.3 A resolution.They crystal belongs to the orthorhombic space group I222, with unit-cell parameters a = 92.69, b = 121.78, c = 77.53 A. Assuming the presence of one molecule per asymmetric unit, the Matthews coefficient V(M) was calculated to be 2.6 A(3) Da(-1) and the solvent content was 53.1% |
684164 |
| 3.4.21.B57 | crystallization of the Pro-S324A/DELTACa6 mutant enzyme using the sitting-drop vapor-diffusion method at 4°C |
726988 |
| 3.4.21.B57 | DeltaCa2-Pro-S324A (Ca2+-binding site Ca 2 is removed) is crystallized using sitting-drop vapor-diffusion method at 4°C. DeltaCa3-Pro-S324A (Ca2+-binding site Ca3 is removed) is crystallized using hanging-drop method at 20°C. The structures of DeltaCa2-Pro-S324A (Ca2+-binding site Ca 2 is removed) and DeltaCa3-Pro-S324A (Ca2+-binding site Ca3 is removed) are identical to that of Pro-S324A, except that they lack the Ca2 and Ca3 sites, respectively, and the structure of the Ca2+-binding loop is destabilized. These proteins are slightly more stable than Pro-S324A. These results suggest that the Ca2+-binding loop is required for folding of Tk-subtilisin but does not seriously contribute to the stabilization of Tk-subtilisin in a native structure. The counting of amino acids refers to the enzyme protein without the signal peptide (amino acid 1-24) and the propeptide (amino acid 25-106) |
707480 |
| 3.4.21.B57 | sitting-drop vapour-diffusion method at 4°C. The crystal structure of the active site mutant of Tk-subtilisin (S324A-subtilisin), which is refolded in the presence of Ca2+ and absence of Tk-propeptide, is determined at 2.16 A resolution. This structure is the same as that of Tk-subtilisin matured from Pro-Tk-subtilisin |
727510 |
| 3.4.21.B57 | sitting-drop, vapor-diffusion method at 20 °C, the crystal structure of the active-site mutant of the proenzyme lacking C-propeptide (ProN-Tk-S359A) is determined at 2.0 A resolution |
728144 |
| 3.4.21.B57 | the crystal structure of Pro-F17H/S324A is nearly identical to that of Pro-S324A, indicating that the mutation does not affect the structure of Pro-Tk-subtilisin |
728762 |
| 3.4.21.B57 | the crystal structure of the complex between L69P-propeptide and S324A-subtilisin (i.e. a protease activity-defective mutant) reveals that the C-terminal region of L69P-propeptide does not well fit into the substrate binding pockets of Tk-subtilisin (S1-S4 subsites) as a result of a conformational change caused by the mutation |
727484 |
