4A54
Structural basis of the Dcp1:Dcp2 mRNA decapping complex activation by Edc3 and Scd6
Summary for 4A54
Entry DOI | 10.2210/pdb4a54/pdb |
Related | 2A6T 4A53 |
NMR Information | BMRB: 18042 |
Descriptor | EDC3, MRNA DECAPPING COMPLEX SUBUNIT 2 (2 entities in total) |
Functional Keywords | rna binding protein-hydrolase complex, rna binding protein/hydrolase |
Biological source | SCHIZOSACCHAROMYCES POMBE (FISSION YEAST) More |
Cellular location | Cytoplasm, P-body: O13828 |
Total number of polymer chains | 2 |
Total formula weight | 15944.78 |
Authors | Fromm, S.A.,Truffault, V.,Kamenz, J.,Braun, J.E.,Hoffmann, N.A.,Izaurralde, E.,Sprangers, R. (deposition date: 2011-10-24, release date: 2012-02-01, Last modification date: 2024-06-19) |
Primary citation | Fromm, S.A.,Truffault, V.,Kamenz, J.,Braun, J.E.,Hoffmann, N.A.,Izaurralde, E.,Sprangers, R. The Structural Basis of Edc3- and Scd6-Mediated Activation of the Dcp1:Dcp2 Mrna Decapping Complex. Embo J., 31:279-, 2011 Cited by PubMed Abstract: The Dcp1:Dcp2 decapping complex catalyses the removal of the mRNA 5' cap structure. Activator proteins, including Edc3 (enhancer of decapping 3), modulate its activity. Here, we solved the structure of the yeast Edc3 LSm domain in complex with a short helical leucine-rich motif (HLM) from Dcp2. The motif interacts with the monomeric Edc3 LSm domain in an unprecedented manner and recognizes a noncanonical binding surface. Based on the structure, we identified additional HLMs in the disordered C-terminal extension of Dcp2 that can interact with Edc3. Moreover, the LSm domain of the Edc3-related protein Scd6 competes with Edc3 for the interaction with these HLMs. We show that both Edc3 and Scd6 stimulate decapping in vitro, presumably by preventing the Dcp1:Dcp2 complex from adopting an inactive conformation. In addition, we show that the C-terminal HLMs in Dcp2 are necessary for the localization of the Dcp1:Dcp2 decapping complex to P-bodies in vivo. Unexpectedly, in contrast to yeast, in metazoans the HLM is found in Dcp1, suggesting that details underlying the regulation of mRNA decapping changed throughout evolution. PubMed: 22085934DOI: 10.1038/EMBOJ.2011.408 PDB entries with the same primary citation |
Experimental method | SOLUTION NMR |
Structure validation
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