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Literature summary for 2.7.7.50 extracted from

  • Kyrieleis, O.J.; Chang, J.; de la Pena, M.; Shuman, S.; Cusack, S.
    Crystal structure of vaccinia virus mRNA capping enzyme provides insights into the mechanism and evolution of the capping apparatus (2014), Structure, 22, 452-465.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

Crystallization (Comment) Organism
structures of the complete heterodimer formed by polypeptides D1 and D12. The D1 subunit comprises an N-terminal RNA triphosphatase (TPase)-guanylyltransferase (GTase) module and a C-terminal guanine-N7-methyltransferase (MTase) module. The D12 subunit binds and allosterically stimulates the MTase module. An extensive TPase-GTase interface clamps the GTase nucleotidyltransferase and oligosaccharide-binding fold domains in a closed conformation around GTP Vaccinia virus

Protein Variants

Protein Variants Comment Organism
E192A 113% of wild-type guanylyltransferase activity, 4% of wild-type RNA triphosphatase activity Vaccinia virus
K478A 1% of wild-type guanylyltransferase activity, 42% of wild-type RNA triphosphatase activity Vaccinia virus
L47A/L50A/T51A 1% of wild-type guanylyltransferase activity, 43% of wild-type RNA triphosphatase activity Vaccinia virus
N181A 48% of wild-type guanylyltransferase activity, 69% of wild-type RNA triphosphatase activity Vaccinia virus
R186A 51% of wild-type guanylyltransferase activity, 92% of wild-type RNA triphosphatase activity Vaccinia virus
T10A 19% of wild-type guanylyltransferase activity, 104% of wild-type RNA triphosphatase activity Vaccinia virus

Organism

Organism UniProt Comment Textmining
Vaccinia virus P04298 mRNA-capping enzyme catalytic subunit
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Vaccinia virus Western Reserve P04298 mRNA-capping enzyme catalytic subunit
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Synonyms

Synonyms Comment Organism
VACWR106
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Vaccinia virus