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Literature summary for 3.4.21.115 extracted from

  • Chung, I.Y.; Paetzel, M.
    Crystal structure of a viral protease intramolecular acyl-enzyme complex: insights into cis-cleavage at the VP4/VP3 junction of Tellina birnavirus (2011), J. Biol. Chem., 286, 12475-12482.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli Tuner (DE3) cells Tellina virus 1

Crystallization (Commentary)

Crystallization (Comment) Organism
VP4 with the C-terminus binding into its own active site forming an intramolecular (cis) acyl-enzyme complex, hanging drop vapor diffusion method, using 21% (w/v) PEG8000 and 0.55 M ammonium sulfate Tellina virus 1

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
24745
-
x * 24745, calculated from amino acid sequence Tellina virus 1

Organism

Organism UniProt Comment Textmining
Tellina virus 1 Q2PBR5 residue 619-830
-

Purification (Commentary)

Purification (Comment) Organism
Ni-NTA column chromatography, SP-Sepharose column chromatography, and Sephacryl S-100 gel filtration Tellina virus 1

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
NH2-pVP2-X-VP4-VP3-COOH + H2O VP4 is encoded as part of the 1114-residue long segment A polyprotein NH2-pVP2-X-VP4-VP3-COOH. It cleaves after amino acid residue positions 512, 618, and 830 to yield capsid precursor protein pVP2, peptide X, VP4 itself, and ribonucleoprotein VP3. Additional cleavage sites were found at the C-terminal side of amino acids 451, 492, and 499 within the pVP2 region Tellina virus 1 pVP2 + peptide X + VP4 + VP3
-
?

Subunits

Subunits Comment Organism
? x * 24745, calculated from amino acid sequence Tellina virus 1

Synonyms

Synonyms Comment Organism
VP4
-
Tellina virus 1

pI Value

Organism Comment pI Value Maximum pI Value
Tellina virus 1 calculated from amino acid sequence
-
9.9