DELTACa2-Pro-S324A |
does not completely lose the ability to fold into a native structure, probably because binding of the water molecule to the position corresponding to the Ca2 site and movement of the epsilon-amino group of Lys213 to the position corresponding to the Ca3 site compensate at least partly for the destabilization of the structure of the Ca2+-binding loop caused by the removal of the Ca2 or Ca3 site |
Thermococcus kodakarensis |
DELTACa3-Pro-S324A |
does not completely lose the ability to fold into a native structure, probably because binding of the water molecule to the position corresponding to the Ca2 site and movement of the epsilon-amino group of Lys213 to the position corresponding to the Ca3 site compensate at least partly for the destabilization of the structure of the Ca2+-binding loop caused by the removal of the Ca2 or Ca3 site |
Thermococcus kodakarensis |
DELTAloop-subtilisin |
the unique insertion sequence of subtilisin (Pro207-Asp226) is removed and Gly206,Ala228, and Glu229 are replaced with Asn, Met, and Asp, respectively. Lacks the Ca2+-binding loop, completely loses the ability to fold into a native structure |
Thermococcus kodakarensis |
S324A |
Pro-S324A represents the active site mutant of pro-subtilisin, Pro-S324A is used to construct mutant proteins to prevent their autoprocessing and self-degradation |
Thermococcus kodakarensis |