2VXG

Crystal structure of the conserved C-terminal region of Ge-1

Summary for 2VXG

• Entry DOI: 10.2210/pdb2vxg/pdb
• Descriptor: CG6181-PA, ISOFORM A (2 entities in total)
• Functional Keywords: decapping, edc4, hedls, mrna decay, p-body, gene regulation
• Biological source: DROSOPHILA MELANOGASTER (FRUIT FLY)
• Cellular location: Cytoplasm, P-body: Q9VKK1
• Total number of polymer chains: 2
• Total formula weight: 31600.46

Authors

Jinek, M.,Eulalio, A.,Lingel, A.,Helms, S.,Conti, E.,Izaurralde, E. (deposition date: 2008-07-04, release date: 2008-09-09, Last modification date: 2024-05-08)

Primary citation

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, 14:1991-, 2008

PubMed Abstract: 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.

PubMed: 18755833
DOI: 10.1261/RNA.1222908

Experimental method

X-RAY DIFFRACTION (1.9 Å)