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| | ==Crystal structure of the conserved C-terminal region of Ge-1== | | ==Crystal structure of the conserved C-terminal region of Ge-1== |
| - | <StructureSection load='2vxg' size='340' side='right' caption='[[2vxg]], [[Resolution|resolution]] 1.90Å' scene=''> | + | <StructureSection load='2vxg' size='340' side='right'caption='[[2vxg]], [[Resolution|resolution]] 1.90Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2vxg]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Drome Drome]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VXG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2VXG FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2vxg]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VXG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2VXG FirstGlance]. <br> |
| - | </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=2vxg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vxg OCA], [http://pdbe.org/2vxg PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2vxg RCSB], [http://www.ebi.ac.uk/pdbsum/2vxg PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2vxg ProSAT]</span></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9Å</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=2vxg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vxg OCA], [https://pdbe.org/2vxg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2vxg RCSB], [https://www.ebi.ac.uk/pdbsum/2vxg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2vxg ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/EDC4_DROME EDC4_DROME] In the process of mRNA degradation, seems to play a role in mRNA decapping. Required for silencing a subset of endogenous miRNA targets.<ref>PMID:17901217</ref> |
| | == 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: Conti, E]] | + | [[Category: Large Structures]] |
| - | [[Category: Eulalio, A]] | + | [[Category: Conti E]] |
| - | [[Category: Helms, S]] | + | [[Category: Eulalio A]] |
| - | [[Category: Izaurralde, E]] | + | [[Category: Helms S]] |
| - | [[Category: Jinek, M]] | + | [[Category: Izaurralde E]] |
| - | [[Category: Lingel, A]] | + | [[Category: Jinek M]] |
| - | [[Category: Decapping]]
| + | [[Category: Lingel A]] |
| - | [[Category: Edc4]]
| + | |
| - | [[Category: Gene regulation]]
| + | |
| - | [[Category: Hedl]]
| + | |
| - | [[Category: Mrna decay]]
| + | |
| - | [[Category: P-body]]
| + | |
| Structural highlights
Function
EDC4_DROME In the process of mRNA degradation, seems to play a role in mRNA decapping. Required for silencing a subset of endogenous miRNA targets.[1]
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
The removal of the 5' cap structure by the DCP1-DCP2 decapping complex irreversibly commits eukaryotic mRNAs to degradation. In human cells, the interaction between DCP1 and DCP2 is bridged by the Ge-1 protein. Ge-1 contains an N-terminal WD40-repeat domain connected by a low-complexity region to a conserved C-terminal domain. It was reported that the C-terminal domain interacts with DCP2 and mediates Ge-1 oligomerization and P-body localization. To understand the molecular basis for these functions, we determined the three-dimensional crystal structure of the most conserved region of the Drosophila melanogaster Ge-1 C-terminal domain. The region adopts an all alpha-helical fold related to ARM- and HEAT-repeat proteins. Using structure-based mutants we identified an invariant surface residue affecting P-body localization. The conservation of critical surface and structural residues suggests that the C-terminal region adopts a similar fold with conserved functions in all members of the Ge-1 protein family.
The C-terminal region of Ge-1 presents conserved structural features required for P-body localization.,Jinek M, Eulalio A, Lingel A, Helms S, Conti E, Izaurralde E RNA. 2008 Oct;14(10):1991-8. Epub 2008 Aug 28. PMID:18755833[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Eulalio A, Rehwinkel J, Stricker M, Huntzinger E, Yang SF, Doerks T, Dorner S, Bork P, Boutros M, Izaurralde E. Target-specific requirements for enhancers of decapping in miRNA-mediated gene silencing. Genes Dev. 2007 Oct 15;21(20):2558-70. PMID:17901217 doi:10.1101/gad.443107
- ↑ Jinek M, Eulalio A, Lingel A, Helms S, Conti E, Izaurralde E. The C-terminal region of Ge-1 presents conserved structural features required for P-body localization. RNA. 2008 Oct;14(10):1991-8. Epub 2008 Aug 28. PMID:18755833 doi:http://dx.doi.org/10.1261/rna.1222908
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