EC Number   |
Reference |
|---|
   3.6.1.62 | apo-form and in complex with IMP and Mg2+, sitting drop vapor diffusion method, using 0.1 MChes pH 9.5 and 20% (w/v) PEG8000 |
758123 |
| 3.6.1.62 | crystallizes as a homodimeric apoenzyme. Structure of X29 complexes with m7GpppA and pppG in the presence of Mn+2 |
716934 |
| 3.6.1.62 | hanging-drop vapour-diffusion method |
713625 |
| 3.6.1.62 | 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 |
733722 |
| 3.6.1.62 | structures of wild-type, and E198Q and E153Q catalytic glutamate mutants of the Dcp2 Nudix domain, to 2.1A, 1.8 A and 1.7 A resolution, respectively. Conserved glutamate residues E152, E153, and E198 coordinate a magnesium ion through a water mediated contact, while E149 directly contacts the metal. A conserved metal binding loop on the catalytic domain undergoes conformational changes during the catalytic cycle |
735287 |
