EC Number   |
|---|
   3.4.21.108 | - |
| 3.4.21.108 | comparison of wild-type and mutan S276C. In wild-type, water molecule number 377 forms an interaction between side chains of S276 and I270* of the adjacent molecule. In mutant S276C, this water molecule is absent |
| 3.4.21.108 | hanging drop vapor diffusion method |
| 3.4.21.108 | structure of the HtrA3 protease domain together with the PDZ domain. The protein forms a trimer |
| 3.4.21.108 | structures of variant V226K/S306A and V325D. Upon binding of specific peptide ligand NH2-GWTMFWV-COOH, the PDZ domains open more dynamically in the wild type protease compared to the V226K mutant, whereas the movement is not observed in the V325D mutant. The movement relies on a PDZ vs. protease domain rotation which opens the protease domain-PDZ interface |
| 3.4.21.108 | to 1.65 A resolution. The catalytic triad in the HtrA2 wild-type structure is disrupted, with the nearest accessible H198 side chain atom positioned 5.9 A away from the carboxylate oxygen of D228 and separated from the hydroxyl of S306 by 7.4 A, requiring substantial rearrangements to reestablish a catalytically competent conformation. Dynamic protein motions are important to HtrA protease activity |
