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Literature summary for 3.4.22.69 extracted from

  • Hu, T.; Zhang, Y.; Li, L.; Wang, K.; Chen, S.; Chen, J.; Ding, J.; Jiang, H.; Shen, X.
    Two adjacent mutations on the dimer interface of SARS coronavirus 3C-like protease cause different conformational changes in crystal structure (2009), Virology, 388, 324-334.
    View publication on PubMed
Search for more literature for 3.4.22.69

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli BL21(DE3) cells SARS coronavirus Tor2

Crystallization (Commentary)

Crystallization (Comment) Organism
hanging drop vapor diffusion method, crystals of S139A mutant are grown from the mother liquor containing 0.1 M MES pH 6.0, 10% (w/v) PEG 6000, 1 mM dithiohtreitol, and 5% (v/v) DMSO, crystals of F140A are grown at three pH values in 0.1 M MES pH 6.0/0.1 M MES pH 6.5/0.1 M Tris pH 7.6, with 10% (w/v) PEG 6000, 1 mM dithiothreitol, and 5% (v/v) DMSO SARS coronavirus Tor2

Protein Variants

Protein Variants Comment Organism
F140A mutant F140A is a dimer with the most collapsed active pocket discovered so far, well-reflecting the stabilizing role of this residue, the mutant enzyme is completely inactive SARS coronavirus Tor2
S139A mutant S139A is a monomer that still retains a small fraction of dimer in solution, which may account for its remaining activity SARS coronavirus Tor2

Organism

Organism UniProt Comment Textmining
SARS coronavirus Tor2 P0C6U8
-
-

Purification (Commentary)

Purification (Comment) Organism
glutathione Sepharose column chromatography and Superdex 75 gel filtration SARS coronavirus Tor2

Subunits

Subunits Comment Organism
homodimer only the dimeric enzyme is active SARS coronavirus Tor2

Synonyms

Synonyms Comment Organism
3C-like protease
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 SARS coronavirus Tor2
3cLpro
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 SARS coronavirus Tor2

General Information

General Information Comment Organism
physiological function 3CLpro is vital for SARS-coronavirus replication SARS coronavirus Tor2