2vxg | pdb_00002vxg
Crystal structure of the conserved C-terminal region of Ge-1
Structural highlights
FunctionEDC4_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 PubMedThe 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
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