Application | Comment | Organism |
---|---|---|
drug development | the enzyme is an attractive target for the development of anti-SARS drugs | Severe acute respiratory syndrome-related coronavirus |
Cloned (Comment) | Organism |
---|---|
recombinant expression of His-tagged mutant R298A enzyme in Escherichia coli strain BL21(DE3) from pET-28a(+) vector | Severe acute respiratory syndrome-related coronavirus |
Crystallization (Comment) | Organism |
---|---|
purified recombinant mutant enzyme R298A with bound substrate, sitting drop vapour diffusion method, mixing of 15 mg/ml protein with substrate TSAVLQ-4-nitroanilide and reservoir solution containing 0.1 M Tris, pH 8.0, 30% w/v PEG 300, 5% w/v PEG 1000, 22°C, 3 days, X-ray diffraction structure determination and analysis at 2.09 A resolution, molecular replacement method | Severe acute respiratory syndrome-related coronavirus |
Protein Variants | Comment | Organism |
---|---|---|
R298A | site-directed mutagenesis, the enzyme mutant shows a reversible substrate-induced dimerization that is essential for catalysis. In substrate-bound mutant enzyme crystals, a dimer with a mutual orientation of the monomers that differs from that of the wild-type protease is present in the asymmetric unit. The presence of a complete substrate-binding pocket and oxyanion hole in both protomers suggests that they are both catalytically active, while the two domain IIIs show minor reorganization. Reorganization of the dimer in the R298A mutant, verview | Severe acute respiratory syndrome-related coronavirus |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Severe acute respiratory syndrome-related coronavirus | P0C6U8 | polyprotein; SARS CoV | - |
Purification (Comment) | Organism |
---|---|
recombinant His-tagged mutant R298A enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography, followed by gel filtration and ultrafiltration | Severe acute respiratory syndrome-related coronavirus |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
pp1a + H2O | cleavage of a viron polyprotein | Severe acute respiratory syndrome-related coronavirus | ? | - |
? | |
pp1ab + H2O | cleavage of a viron polyprotein | Severe acute respiratory syndrome-related coronavirus | ? | - |
? | |
TSAVLQ-4-nitroanilide + H2O | - |
Severe acute respiratory syndrome-related coronavirus | TSAVLQ + 4-nitroaniline | - |
? |
Subunits | Comment | Organism |
---|---|---|
homodimer | the coronaviral enzyme consists of three domains and the catalytic dyad His/Cys is located at the interface between domains I and II. The first two domains have an antiparallel beta-barrel structure that forms a folding scaffold similar to other viral chymotrypsin-like proteases. The functional unit of Mpro is a homodimer and each subunit contains a His41-Cys145 catalytic dyad | Severe acute respiratory syndrome-related coronavirus |
More | molecular mechanism of substrate-induced dimerization, overview | Severe acute respiratory syndrome-related coronavirus |
Synonyms | Comment | Organism |
---|---|---|
3cLpro | - |
Severe acute respiratory syndrome-related coronavirus |
SARS coronavirus main protease | - |
Severe acute respiratory syndrome-related coronavirus |
SARS coronavirus Mpro | - |
Severe acute respiratory syndrome-related coronavirus |
SARSCoV main protease | - |
Severe acute respiratory syndrome-related coronavirus |
SARSCoV Mpro | - |
Severe acute respiratory syndrome-related coronavirus |
severe acute respiratory syndrome coronavirus main protease | - |
Severe acute respiratory syndrome-related coronavirus |
severe acute respiratory syndrome coronavirus Mpro | - |
Severe acute respiratory syndrome-related coronavirus |
General Information | Comment | Organism |
---|---|---|
additional information | the functional unit of Mpro is a homodimer and each subunit contains a His41-Cys145 catalytic dyad. Presence of a complete substrate-binding pocket and oxyanion hole in both protomers. Reversible substrate-induced dimerization is essential for catalysis, molecular mechanism, overview | Severe acute respiratory syndrome-related coronavirus |