2rm4: Difference between revisions

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{{Seed}}
[[Image:2rm4.png|left|200px]]


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==Solution Structure of the LSM Domain of Dm EDC3 (Enhancer of DECAPPING 3)==
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<StructureSection load='2rm4' size='340' side='right'caption='[[2rm4]]' scene=''>
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== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<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>
or leave the SCENE parameter empty for the default display.
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
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<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>
{{STRUCTURE_2rm4|  PDB=2rm4  |  SCENE=  }}
</table>
== Function ==
[https://www.uniprot.org/uniprot/EDC3_DROME EDC3_DROME] In the process of mRNA degradation, may play a role in mRNA decapping.
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/rm/2rm4_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2rm4 ConSurf].
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== 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.


===Solution Structure of the LSM Domain of Dm EDC3 (Enhancer of DECAPPING 3)===
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<ref>PMID:17923697</ref>


 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 2rm4" style="background-color:#fffaf0;"></div>
(as it appears on PubMed at http://www.pubmed.gov), where 17923697 is the PubMed ID number.
== References ==
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<references/>
{{ABSTRACT_PUBMED_17923697}}
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</StructureSection>
==About this Structure==
2RM4 is a [[Single protein]] structure of sequence from [http://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].
 
==Reference==
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:[http://www.ncbi.nlm.nih.gov/pubmed/17923697 17923697]
[[Category: Drosophila melanogaster]]
[[Category: Drosophila melanogaster]]
[[Category: Single protein]]
[[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]]
[[Category: Protein binding]]
[[Category: Sm-like protein]]
 
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Retrieved from "https://proteopedia.org/2rm4"