3D3J
Crystal structure of human Edc3p
Summary for 3D3J
| Entry DOI | 10.2210/pdb3d3j/pdb |
| Related | 3D3K |
| Descriptor | Enhancer of mRNA-decapping protein 3 (2 entities in total) |
| Functional Keywords | hedc3, phosphoprotein, protein binding |
| Biological source | Homo sapiens (human) |
| Cellular location | Cytoplasm, P-body: Q96F86 |
| Total number of polymer chains | 1 |
| Total formula weight | 34170.10 |
| Authors | Ling, S.H.M. (deposition date: 2008-05-12, release date: 2008-08-26, Last modification date: 2023-11-01) |
| Primary citation | Ling, S.H.M.,Decker, C.J.,Walsh, M.A.,She, M.,Parker, R.,Song, H. Crystal structure of human Edc3 and its functional implications Mol.Cell.Biol., 28:5965-5976, 2008 Cited by PubMed Abstract: Edc3 is an enhancer of decapping and serves as a scaffold that aggregates mRNA ribonucleoproteins together for P-body formation. Edc3 forms a network of interactions with the components of the mRNA decapping machinery and has a modular domain architecture consisting of an N-terminal Lsm domain, a central FDF domain, and a C-terminal YjeF-N domain. We have determined the crystal structure of the N-terminally truncated human Edc3 at a resolution of 2.2 A. The structure reveals that the YjeF-N domain of Edc3 possesses a divergent Rossmann fold topology that forms a dimer, which is supported by sedimentation velocity and sedimentation equilibrium analysis in solution. The dimerization interface of Edc3 is highly conserved in eukaryotes despite the overall low sequence homology across species. Structure-based site-directed mutagenesis revealed dimerization is required for efficient RNA binding, P-body formation, and likely for regulating the yeast Rps28B mRNA as well, suggesting that the dimeric form of Edc3 is a structural and functional unit in mRNA degradation. PubMed: 18678652DOI: 10.1128/MCB.00761-08 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.8 Å) |
Structure validation
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