4a53: Difference between revisions
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==Structural basis of the Dcp1:Dcp2 mRNA decapping complex activation by Edc3 and Scd6== | ==Structural basis of the Dcp1:Dcp2 mRNA decapping complex activation by Edc3 and Scd6== | ||
<StructureSection load='4a53' size='340' side='right'caption='[[4a53 | <StructureSection load='4a53' size='340' side='right'caption='[[4a53]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4a53]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[4a53]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Schizosaccharomyces_pombe Schizosaccharomyces pombe]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4A53 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4A53 FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4a53 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4a53 OCA], [https://pdbe.org/4a53 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4a53 RCSB], [https://www.ebi.ac.uk/pdbsum/4a53 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4a53 ProSAT]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4a53 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4a53 OCA], [https://pdbe.org/4a53 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4a53 RCSB], [https://www.ebi.ac.uk/pdbsum/4a53 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4a53 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/EDC3_SCHPO EDC3_SCHPO] Stimulates decapping of both stable and unstable mRNA during mRNA decay. Stimulates decapping presumably by preventing the DCP1-DCP2 decapping complex from adopting an inactive conformation.<ref>PMID:22085934</ref> | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Braun | [[Category: Schizosaccharomyces pombe]] | ||
[[Category: Fromm | [[Category: Braun JE]] | ||
[[Category: Hoffmann | [[Category: Fromm SA]] | ||
[[Category: Izaurralde | [[Category: Hoffmann NA]] | ||
[[Category: Kamenz | [[Category: Izaurralde E]] | ||
[[Category: Sprangers | [[Category: Kamenz J]] | ||
[[Category: Truffault | [[Category: Sprangers R]] | ||
[[Category: Truffault V]] | |||
Latest revision as of 09:00, 19 June 2024
Structural basis of the Dcp1:Dcp2 mRNA decapping complex activation by Edc3 and Scd6Structural basis of the Dcp1:Dcp2 mRNA decapping complex activation by Edc3 and Scd6
Structural highlights
FunctionEDC3_SCHPO Stimulates decapping of both stable and unstable mRNA during mRNA decay. Stimulates decapping presumably by preventing the DCP1-DCP2 decapping complex from adopting an inactive conformation.[1] Publication Abstract from PubMedThe 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. The structural basis of Edc3- and Scd6-mediated activation of the Dcp1:Dcp2 mRNA decapping complex.,Fromm SA, Truffault V, Kamenz J, Braun JE, Hoffmann NA, Izaurralde E, Sprangers R EMBO J. 2011 Nov 15;31(2):279-90. doi: 10.1038/emboj.2011.408. PMID:22085934[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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