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Literature summary for 2.7.7.19 extracted from

  • Moure, C.M.; Bowman, B.R.; Gershon, P.D.; Quiocho, F.A.
    Crystal structures of the vaccinia virus polyadenylate polymerase heterodimer: insights into ATP selectivity and processivity (2006), Mol. Cell, 22, 339-349.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
ATP-gamma-S bound and unbound structures. Subunit VP55 residues of the active site make specific interactions with ATP-gamma-S. Concave surface of subunit VP55 docks the globular subunit VP39. Model of RNA primer binding shows that subunit VP39 functions as a processivity factor by partially enclosing the RNA primer at the heterodimer interface Vaccinia virus

Organism

Organism UniProt Comment Textmining
Vaccinia virus
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