F34A |
site-directed mutagenesis |
Staphylococcus aureus |
I92A |
site-directed mutagenesis, the mutant shows similar global stability like the wild-type enzyme |
Staphylococcus aureus |
L103A |
site-directed mutagenesis, the mutant shows similar global stability like the wild-type enzyme |
Staphylococcus aureus |
L125A |
site-directed mutagenesis, the mutant shows similar global stability like the wild-type enzyme |
Staphylococcus aureus |
L25A |
site-directed mutagenesis |
Staphylococcus aureus |
L36A |
site-directed mutagenesis |
Staphylococcus aureus |
L38A |
site-directed mutagenesis |
Staphylococcus aureus |
additional information |
ten cavity-containing variants of the highly stable form of the enzyme known as DELTA+PHS SNase are described, the DELTA+ PHS reference protein bears stabilizing substitutions in the C-terminal helix (G50F, V51N, P117G, H124L, and S128A), and a deletion of the mobile X loop (residues 44-49), which is part of the active site. Variants with substitutions in the C-terminal domain and the interface between alpha and beta subdomains showed large amide chemical shift variations relative to the parent protein, moderate, widespread, and compensatory perturbations of the H/D protection factors and increased local dynamics on a nanosecond time scale. In contrast, cavity creation in the beta-barrel subdomain leads to minimal perturbation of the structure of the folded state |
Staphylococcus aureus |
V23A |
site-directed mutagenesis |
Staphylococcus aureus |
V66A |
site-directed mutagenesis, the mutant shows similar global stability like the wild-type enzyme |
Staphylococcus aureus |
V74A |
site-directed mutagenesis |
Staphylococcus aureus |