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Literature summary for 3.4.22.69 extracted from

  • Shi, J.; Sivaraman, J.; Song, J.
    Mechanism for controlling the dimer-monomer switch and coupling dimerization to catalysis of the severe acute respiratory syndrome coronavirus 3C-like protease (2008), J. Virol., 82, 4620-4629.
    View publication on PubMedView publication on EuropePMC
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Cloned(Commentary)

Cloned (Comment) Organism
R298A protease is expressed in Escherichia coli strain BL21(DE3) Severe acute respiratory syndrome-related coronavirus

Crystallization (Commentary)

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

Protein Variants Comment Organism
R298A monomeric mutant Severe acute respiratory syndrome-related coronavirus

Organism

Organism UniProt Comment Textmining
Severe acute respiratory syndrome-related coronavirus
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-
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Subunits

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

Synonyms Comment Organism
severe acute respiratory syndrome coronavirus 3C-like protease
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 Severe acute respiratory syndrome-related coronavirus