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Literature summary for 3.4.22.46 extracted from

  • Zunszain, P.A.; Knox, S.R.; Sweeney, T.R.; Yang, J.; Roque-Rosell, N.; Belsham, G.J.; Leatherbarrow, R.J.; Curry, S.
    Insights into cleavage specificity from the crystal structure of foot-and-mouth disease virus 3C protease complexed with a peptide substrate (2010), J. Mol. Biol., 395, 375-389.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression of enzyme mutants in Escherichia coli Foot-and-mouth disease virus

Crystallization (Commentary)

Crystallization (Comment) Organism
foot-and-mouth disease virus 3C protease mutant C95K/C142L/C163A complexed with a peptide substrates APAKQLLNFD and APAKELLNFD that spans P5-P5', 1:5.5 molar ratio of enzyme to peptide, 0.05 ml of of 3Cpro solution at 17 mg/ml protein in 100 mM HEPES, pH 7.0, 400 mM NaCl, 1 mM EDTA, 2 mM 2-mercaptoethanol, and 0.01% w/v sodium azide is mixed with 0.007 ml of 30 mM peptide dissolved in the same buffer, yielding a final protein concentration of 14.9 mg/ml, sitting-drop vapour diffusion, room temperature, mixing of 0.001 ml of protein complex solution with 0.003 ml reservoir composed of 40-43% PEG 400, 0.2 M LiSO4 and 0.1 M Tris, pH 8.0 X-ray diffraction structure determination and analysis Foot-and-mouth disease virus

Protein Variants

Protein Variants Comment Organism
C95K/C142L/C163A the C-terminally truncated, catalytically inactive mutant has wild-type binding activity but remains soluble at purified protein concentrations in excess of 10 mg/ml Foot-and-mouth disease virus
C95K/C142S/C163A C-terminally truncated, catalytically inactive form of the type A10FMDV 3Cpro Foot-and-mouth disease virus

Organism

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

Purification (Commentary)

Purification (Comment) Organism
recombinant enzyme mutants from Escherichia coli by gel filtration Foot-and-mouth disease virus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information the enzyme typically recognise the alternating positions of the side chains along the polypeptide sequence that are characteristic of an extended backbone conformation, and this serves to place the scissile bond in the correct orientation at the active site. Significant conformational adaptation by the enzyme is important for substrate recognition Foot-and-mouth disease virus ?
-
?

Subunits

Subunits Comment Organism
More the peptide binding cleft, which contains the active site at its centre, is located at the interface between two beta-barrels. Unusually, picornaviral 3Cpro possess a Cys-His-Asp/Glu catalytic triad at the centre of this cleft, instead of the Ser-His-Asp arrangement of active-site residues Foot-and-mouth disease virus

Synonyms

Synonyms Comment Organism
FMDV 3Cpro
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Foot-and-mouth disease virus
foot-and-mouth disease virus 3C protease
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Foot-and-mouth disease virus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
assay at Foot-and-mouth disease virus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.1
-
assay at Foot-and-mouth disease virus

General Information

General Information Comment Organism
evolution significant conformational adaptation by the enzyme is important for substrate recognition, specificity differences between 3Cpro from different picornaviruses, overview Foot-and-mouth disease virus
physiological function the viral RNA genome is translated in the cytoplasm of infected cells as a long polyprotein precursor that is cleaved by virally encoded proteases to release functional proteins needed for the synthesis of new virions. In 10 of 13 cases, 3Cpro performs the cleavages by targeting specific sequences within the polyprotein Foot-and-mouth disease virus