Cloned (Comment) | Organism |
---|---|
R298A protease is expressed in Escherichia coli strain BL21(DE3) | Severe acute respiratory syndrome-related coronavirus |
Crystallization (Comment) | Organism |
---|---|
monomeric crystal structure of the SARS-CoV 3CLpro mutant R298A at a resolution of 1.75 A, hanging drop method | Severe acute respiratory syndrome-related coronavirus |
Protein Variants | Comment | Organism |
---|---|---|
R298A | monomeric mutant | Severe acute respiratory syndrome-related coronavirus |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Severe acute respiratory syndrome-related coronavirus | - |
- |
- |
Subunits | Comment | Organism |
---|---|---|
dimer | is only enzymatically active as a homodimer. Arg298 serves as a key component for maintaining dimerization, and consequently, its mutation will trigger a cooperative switch from a dimer to a monomer. The monomeric enzyme is irreversibly inactivated because its catalytic machinery is frozen in the collapsed state, characteristic of the formation of a short 310-helix from an active-site loop. Dimerization appears to be coupled to catalysis in 3CLpro through the use of overlapped residues for two networks, one for dimerization and another for the catalysis | Severe acute respiratory syndrome-related coronavirus |
Synonyms | Comment | Organism |
---|---|---|
severe acute respiratory syndrome coronavirus 3C-like protease | - |
Severe acute respiratory syndrome-related coronavirus |