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| | ==Solution Structure of the LSM Domain of Dm EDC3 (Enhancer of DECAPPING 3)== | | ==Solution Structure of the LSM Domain of Dm EDC3 (Enhancer of DECAPPING 3)== |
| - | <StructureSection load='2rm4' size='340' side='right'caption='[[2rm4]], [[NMR_Ensembles_of_Models | 22 NMR models]]' scene=''> | + | <StructureSection load='2rm4' size='340' side='right'caption='[[2rm4]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2rm4]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Drome Drome]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RM4 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=2RM4 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2rm4]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RM4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2RM4 FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2vc8|2vc8]]</td></tr> | + | </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'>[http://proteopedia.org/fgij/fg.htm?mol=2rm4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2rm4 OCA], [http://pdbe.org/2rm4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2rm4 RCSB], [http://www.ebi.ac.uk/pdbsum/2rm4 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2rm4 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=2rm4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2rm4 OCA], [https://pdbe.org/2rm4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2rm4 RCSB], [https://www.ebi.ac.uk/pdbsum/2rm4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2rm4 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/EDC3_DROME EDC3_DROME]] In the process of mRNA degradation, may play a role in mRNA decapping. | + | [https://www.uniprot.org/uniprot/EDC3_DROME EDC3_DROME] In the process of mRNA degradation, may play a role in mRNA decapping. |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Drome]] | + | [[Category: Drosophila melanogaster]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Coles, M]] | + | [[Category: Coles M]] |
| - | [[Category: Tritschler, F]] | + | [[Category: Tritschler F]] |
| - | [[Category: Truffault, V]] | + | [[Category: Truffault V]] |
| - | [[Category: Enhancer of mrna decapping]]
| + | |
| - | [[Category: P-body component]]
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| - | [[Category: Protein binding]]
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| - | [[Category: Sm-like protein]]
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| Structural highlights
Function
EDC3_DROME In the process of mRNA degradation, may play a role in mRNA decapping.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Members of the (L)Sm (Sm and Sm-like) protein family are found across all kingdoms of life and play crucial roles in RNA metabolism. The P-body component EDC3 (enhancer of decapping 3) is a divergent member of this family that functions in mRNA decapping. EDC3 is composed of a N-terminal LSm domain, a central FDF domain, and a C-terminal YjeF-N domain. We show that this modular architecture enables EDC3 to interact with multiple components of the decapping machinery, including DCP1, DCP2, and Me31B. The LSm domain mediates DCP1 binding and P-body localization. We determined the three-dimensional structures of the LSm domains of Drosophila melanogaster and human EDC3 and show that the domain adopts a divergent Sm fold that lacks the characteristic N-terminal alpha-helix and has a disrupted beta4-strand. This domain remains monomeric in solution and lacks several features that canonical (L)Sm domains require for binding RNA. The structures also revealed a conserved patch of surface residues that are required for the interaction with DCP1 but not for P-body localization. The conservation of surface and of critical structural residues indicates that LSm domains in EDC3 proteins adopt a similar fold that has separable novel functions that are absent in canonical (L)Sm proteins.
A divergent Sm fold in EDC3 proteins mediates DCP1 binding and P-body targeting.,Tritschler F, Eulalio A, Truffault V, Hartmann MD, Helms S, Schmidt S, Coles M, Izaurralde E, Weichenrieder O Mol Cell Biol. 2007 Dec;27(24):8600-11. Epub 2007 Oct 8. PMID:17923697[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Tritschler F, Eulalio A, Truffault V, Hartmann MD, Helms S, Schmidt S, Coles M, Izaurralde E, Weichenrieder O. A divergent Sm fold in EDC3 proteins mediates DCP1 binding and P-body targeting. Mol Cell Biol. 2007 Dec;27(24):8600-11. Epub 2007 Oct 8. PMID:17923697 doi:10.1128/MCB.01506-07
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