2rm4
From Proteopedia
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Solution Structure of the LSM Domain of Dm EDC3 (Enhancer of DECAPPING 3)
Overview
Members of the (L)Sm (Sm and Like-Sm) 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.
About this Structure
2RM4 is a Single protein structure of sequence from Drosophila melanogaster. Full crystallographic information is available from OCA.
Reference
A divergent Sm-fold in EDC3 proteins mediates DCP1-binding and P-body targeting., Tritschler F, Eulalio A, Truffault V, Hartmann MD, Helms S, Schmidt S, Coles M, Izaurralde E, Weichenrieder O, Mol Cell Biol. 2007 Oct 8;. PMID:17923697
Page seeded by OCA on Wed Jan 23 11:18:34 2008
