2RM4

Solution Structure of the LSM Domain of Dm EDC3 (Enhancer of DECAPPING 3)

2RM4 の概要

• エントリーDOI: 10.2210/pdb2rm4/pdb
• 関連するPDBエントリー: 2vc8
• NMR情報: BMRB: 11009
• 分子名称: CG6311-PB (1 entity in total)
• 機能のキーワード: enhancer of mrna decapping, p-body component, sm-like protein, protein binding
• 由来する生物種: Drosophila melanogaster (fruit fly)
• 細胞内の位置: Cytoplasm, P-body: Q9VVI2
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 11095.80

構造登録者

Truffault, V.,Coles, M.,Tritschler, F. (登録日: 2007-09-20, 公開日: 2007-10-30, 最終更新日: 2024-05-29)

主引用文献

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

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: 17923697
DOI: 10.1128/MCB.01506-07

実験手法

SOLUTION NMR