2RM4
Solution Structure of the LSM Domain of Dm EDC3 (Enhancer of DECAPPING 3)
Summary for 2RM4
| Entry DOI | 10.2210/pdb2rm4/pdb |
| Related | 2vc8 |
| NMR Information | BMRB: 11009 |
| Descriptor | CG6311-PB (1 entity in total) |
| Functional Keywords | enhancer of mrna decapping, p-body component, sm-like protein, protein binding |
| Biological source | Drosophila melanogaster (fruit fly) |
| Cellular location | Cytoplasm, P-body: Q9VVI2 |
| Total number of polymer chains | 1 |
| Total formula weight | 11095.80 |
| Authors | Truffault, V.,Coles, M.,Tritschler, F. (deposition date: 2007-09-20, release date: 2007-10-30, Last modification date: 2024-05-29) |
| Primary citation | Tritschler, F.,Eulalio, A.,Truffault, V.,Hartmann, M.D.,Helms, S.,Schmidt, S.,Coles, M.,Izaurralde, E.,Weichenrieder, O. A divergent Sm fold in EDC3 proteins mediates DCP1 binding and P-body targeting Mol.Cell.Biol., 27:8600-8611, 2007 Cited by PubMed Abstract: Members of the (L)Sm (Sm and Sm-like) protein family are found across all kingdoms of life and play crucial roles in RNA metabolism. The P-body component EDC3 (enhancer of decapping 3) is a divergent member of this family that functions in mRNA decapping. EDC3 is composed of a N-terminal LSm domain, a central FDF domain, and a C-terminal YjeF-N domain. We show that this modular architecture enables EDC3 to interact with multiple components of the decapping machinery, including DCP1, DCP2, and Me31B. The LSm domain mediates DCP1 binding and P-body localization. We determined the three-dimensional structures of the LSm domains of Drosophila melanogaster and human EDC3 and show that the domain adopts a divergent Sm fold that lacks the characteristic N-terminal alpha-helix and has a disrupted beta4-strand. This domain remains monomeric in solution and lacks several features that canonical (L)Sm domains require for binding RNA. The structures also revealed a conserved patch of surface residues that are required for the interaction with DCP1 but not for P-body localization. The conservation of surface and of critical structural residues indicates that LSm domains in EDC3 proteins adopt a similar fold that has separable novel functions that are absent in canonical (L)Sm proteins. PubMed: 17923697DOI: 10.1128/MCB.01506-07 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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