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Literature summary for 3.4.22.45 extracted from

  • Plisson, C.; Drucker, M.; Blanc, S.; German-Retana, S.; Le Gall, O.; Thomas, D.; Bron, P.
    Structural characterization of HC-Pro, a plant virus multifunctional protein (2003), J. Biol. Chem., 278, 23753-23761.
    View publication on PubMed
Search for more literature for 3.4.22.45

Crystallization (Commentary)

Crystallization (Comment) Organism
two-dimensional crystal of the recombinant proteins are successfully grown on Ni2+-chelating lipid monolayxers. Comparison of projection maps of negatively stained crystals reveal that the enzyme is composed of two domains separated by a flexible constriction lettuce mosaic virus

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
53000
-
 2 * 53000, the enzyme is a dimer in solution, the N-terminus is not essential for self-interaction, SDS-PAGE lettuce mosaic virus
138000
-
 gel filtration lettuce mosaic virus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information lettuce mosaic virus the enzyme is involved in different steps of the viral cycle, aphid transmission, replication, and virus cell-to-cell and systemic movement and is a suppressor of posttranscriptional gene silencing ?
-
 ?

Organism

Organism UniProt Comment Textmining
lettuce mosaic virus
-
-
-

Purification (Commentary)

Purification (Comment) Organism
His-tagged wild-type enzyme and an N-terminal deletion mutant lettuce mosaic virus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information the enzyme is involved in different steps of the viral cycle, aphid transmission, replication, and virus cell-to-cell and systemic movement and is a suppressor of posttranscriptional gene silencing lettuce mosaic virus ?
-
 ?

Subunits

Subunits Comment Organism
dimer 2 * 53000, the enzyme is a dimer in solution, the N-terminus is not essential for self-interaction, SDS-PAGE lettuce mosaic virus