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Literature summary for 3.6.1.62 extracted from

  • Fromm, S.; Truffault, V.; Kamenz, J.; Braun, J.; Hoffmann, N.; Izaurralde, E.; Sprangers, R.
    The structural basis of Edc3-and Scd6-mediated activation of the Dcp1:Dcp2 mRNA decapping complex (2012), EMBO J., 31, 279-290.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

Crystallization (Comment) Organism
structure of the yeast enhancer of mRNA-decapping protein Edc3 LSm domain in complex with a short helical leucine-rich motif from subunit Dcp2. The motif interacts with the monomeric Edc3 LSm domain and recognizes a noncanonical binding surface. Additional helical leucine-rich motifs in the disordered C-terminal extension of Dcp2 can interact with Edc3. Both Edc3 and Scd6 stimulate decapping in vitro, presumably by preventing the Dcp1:Dcp2 complex from adopting an inactive conformation. The C-terminal helical leucine-rich motifs in Dcp2 are necessary for the localization of the Dcp1:Dcp2 decapping complex to P-bodies in vivo Schizosaccharomyces pombe

Organism

Organism UniProt Comment Textmining
Schizosaccharomyces pombe O13828
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Schizosaccharomyces pombe ATCC 24843 O13828
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