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Literature summary for 3.4.22.28 extracted from

  • Sweeney, T.R.; Roque-Rosell, N.; Birtley, J.R.; Leatherbarrow, R.J.; Curry, S.
    Structural and mutagenic analysis of foot-and-mouth disease virus 3C protease reveals the role of the beta-ribbon in proteolysis (2007), J. Virol., 81, 115-124.
    View publication on PubMedView publication on EuropePMC
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Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli BL21(DE3) cells Foot-and-mouth disease virus

Crystallization (Commentary)

Crystallization (Comment) Organism
sitting drop vapour diffusion method with 16 to 22% polyethylene glycol 4000, 100 mM Tris HCl (pH 8.5), and 2 mM sodium acetate Foot-and-mouth disease virus

Protein Variants

Protein Variants Comment Organism
C142A mutant shows reduced activity Foot-and-mouth disease virus
C142L mutant shows increased activity Foot-and-mouth disease virus
C142S mutation has no effect onsubstrate specificity but drastically reduces the proteolytic activity of the enzyme to less than 1% of the wild type activity Foot-and-mouth disease virus
C142T mutant shows reduced activity Foot-and-mouth disease virus
C142V mutant shows reduced activity Foot-and-mouth disease virus
C95K/C142S both mutations are required to make the recombinant enzyme soluble Foot-and-mouth disease virus

Organism

Organism UniProt Comment Textmining
Foot-and-mouth disease virus
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-
-
Foot-and-mouth disease virus A1061
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-
-

Purification (Commentary)

Purification (Comment) Organism
TALON resin chromatography and by gel filtration Foot-and-mouth disease virus

Synonyms

Synonyms Comment Organism
3C protease
-
 Foot-and-mouth disease virus
3Cpro a chymotrypsin-like cysteine protease Foot-and-mouth disease virus