4a54

From Proteopedia

(Difference between revisions)

Revision as of 07:45, 18 August 2022

Structural basis of the Dcp1:Dcp2 mRNA decapping complex activation by Edc3 and Scd6

Structural highlights

4a54 is a 2 chain structure with sequence from Cbs 356. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Related:	2a6t, 4a53
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[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.^[1] [DCP2_SCHPO] Catalytic component of the decapping complex necessary for the degradation of mRNAs, both in normal mRNA turnover and in nonsense-mediated mRNA decay. Removes the 7-methyl guanine cap structure from mRNA molecules, yielding a 5'-phosphorylated mRNA fragment and 7m-GDP. Decapping is the major pathway of mRNA degradation in yeast. It occurs through deadenylation, decapping and subsequent 5' to 3' exonucleolytic decay of the transcript body.^[2]

Publication Abstract from PubMed

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.

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^[3]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Fromm SA, Truffault V, Kamenz J, Braun JE, Hoffmann NA, Izaurralde E, Sprangers R. The structural basis of Edc3- and Scd6-mediated activation of the Dcp1:Dcp2 mRNA decapping complex. EMBO J. 2011 Nov 15;31(2):279-90. doi: 10.1038/emboj.2011.408. PMID:22085934 doi:10.1038/emboj.2011.408
↑ Sakuno T, Araki Y, Ohya Y, Kofuji S, Takahashi S, Hoshino S, Katada T. Decapping reaction of mRNA requires Dcp1 in fission yeast: its characterization in different species from yeast to human. J Biochem. 2004 Dec;136(6):805-12. PMID:15671491 doi:http://dx.doi.org/136/6/805
↑ Fromm SA, Truffault V, Kamenz J, Braun JE, Hoffmann NA, Izaurralde E, Sprangers R. The structural basis of Edc3- and Scd6-mediated activation of the Dcp1:Dcp2 mRNA decapping complex. EMBO J. 2011 Nov 15;31(2):279-90. doi: 10.1038/emboj.2011.408. PMID:22085934 doi:10.1038/emboj.2011.408

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4a54"

@@ Line 3: / Line 3: @@
 <StructureSection load='4a54' size='340' side='right'caption='[[4a54]], [[NMR_Ensembles_of_Models | 22 NMR models]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[4a54]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Cbs_356 Cbs 356]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4A54 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4A54 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[4a54]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Cbs_356 Cbs 356]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4A54 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4A54 FirstGlance]. <br>
-</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2a6t|2a6t]], [[4a53|4a53]]</td></tr>
+</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2a6t|2a6t]], [[4a53|4a53]]</div></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4a54 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4a54 OCA], [http://pdbe.org/4a54 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4a54 RCSB], [http://www.ebi.ac.uk/pdbsum/4a54 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4a54 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=4a54 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4a54 OCA], [https://pdbe.org/4a54 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4a54 RCSB], [https://www.ebi.ac.uk/pdbsum/4a54 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4a54 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://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>  [[http://www.uniprot.org/uniprot/DCP2_SCHPO DCP2_SCHPO]] Catalytic component of the decapping complex necessary for the degradation of mRNAs, both in normal mRNA turnover and in nonsense-mediated mRNA decay. Removes the 7-methyl guanine cap structure from mRNA molecules, yielding a 5'-phosphorylated mRNA fragment and 7m-GDP. Decapping is the major pathway of mRNA degradation in yeast. It occurs through deadenylation, decapping and subsequent 5' to 3' exonucleolytic decay of the transcript body.<ref>PMID:15671491</ref>
+[[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>  [[https://www.uniprot.org/uniprot/DCP2_SCHPO DCP2_SCHPO]] Catalytic component of the decapping complex necessary for the degradation of mRNAs, both in normal mRNA turnover and in nonsense-mediated mRNA decay. Removes the 7-methyl guanine cap structure from mRNA molecules, yielding a 5'-phosphorylated mRNA fragment and 7m-GDP. Decapping is the major pathway of mRNA degradation in yeast. It occurs through deadenylation, decapping and subsequent 5' to 3' exonucleolytic decay of the transcript body.<ref>PMID:15671491</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 23: / Line 23: @@
 </StructureSection>
 [[Category: Cbs 356]]
+[[Category: Large Structures]]
 [[Category: Braun, J E]]
 [[Category: Fromm, S A]]

4a54

From Proteopedia

Revision as of 07:45, 18 August 2022

Structural basis of the Dcp1:Dcp2 mRNA decapping complex activation by Edc3 and Scd6

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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