This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.

2wx4

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Current revision

Asymmetric trimer of the Drosophila melanogaster DCP1 C-terminal domain

Structural highlights

2wx4 is a 6 chain structure with sequence from Drosophila melanogaster. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.8Å
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

Q9W1H5_DROME

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

DCP1 stimulates the decapping enzyme DCP2, which removes the mRNA 5' cap structure committing mRNAs to degradation. In multicellular eukaryotes, DCP1-DCP2 interaction is stabilized by additional proteins, including EDC4. However, most information on DCP2 activation stems from studies in S. cerevisiae, which lacks EDC4. Furthermore, DCP1 orthologs from multicellular eukaryotes have a C-terminal extension, absent in fungi. Here, we show that in metazoa, a conserved DCP1 C-terminal domain drives DCP1 trimerization. Crystal structures of the DCP1-trimerization domain reveal an antiparallel assembly comprised of three kinked alpha-helices. Trimerization is required for DCP1 to be incorporated into active decapping complexes and for efficient mRNA decapping in vivo. Our results reveal an unexpected connectivity and complexity of the mRNA decapping network in multicellular eukaryotes, which likely enhances opportunities for regulating mRNA degradation.

DCP1 forms asymmetric trimers to assemble into active mRNA decapping complexes in metazoa.,Tritschler F, Braun JE, Motz C, Igreja C, Haas G, Truffault V, Izaurralde E, Weichenrieder O Proc Natl Acad Sci U S A. 2009 Dec 4. PMID:19966221^[1]

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

References

↑ Tritschler F, Braun JE, Motz C, Igreja C, Haas G, Truffault V, Izaurralde E, Weichenrieder O. DCP1 forms asymmetric trimers to assemble into active mRNA decapping complexes in metazoa. Proc Natl Acad Sci U S A. 2009 Dec 4. PMID:19966221

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2wx4"

Categories: Drosophila melanogaster | Large Structures | Tritschler F | Weichenrieder O

@@ Line 3: / Line 3: @@
 <StructureSection load='2wx4' size='340' side='right'caption='[[2wx4]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2wx4]] is a 6 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=2WX4 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=2WX4 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2wx4]] is a 6 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=2WX4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2WX4 FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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]] 2.8&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2wx3|2wx3]]</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=2wx4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2wx4 OCA], [http://pdbe.org/2wx4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2wx4 RCSB], [http://www.ebi.ac.uk/pdbsum/2wx4 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2wx4 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=2wx4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2wx4 OCA], [https://pdbe.org/2wx4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2wx4 RCSB], [https://www.ebi.ac.uk/pdbsum/2wx4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2wx4 ProSAT]</span></td></tr>
 </table>
+== Function ==
+[https://www.uniprot.org/uniprot/Q9W1H5_DROME Q9W1H5_DROME]
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 31: / Line 33: @@
 __TOC__
 </StructureSection>
-[[Category: Drome]]
+[[Category: Drosophila melanogaster]]
 [[Category: Large Structures]]
-[[Category: Tritschler, F]]
+[[Category: Tritschler F]]
-[[Category: Weichenrieder, O]]
+[[Category: Weichenrieder O]]
-[[Category: Asymmetric assembly]]
-[[Category: Mrna decapping]]
-[[Category: P-body component]]
-[[Category: Structural protein]]
-[[Category: Trimerization module]]

2wx4

From Proteopedia

Current revision

Asymmetric trimer of the Drosophila melanogaster DCP1 C-terminal domain

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox