3D3K

Crystal structure of human Edc3p

3D3K の概要

• エントリーDOI: 10.2210/pdb3d3k/pdb
• 関連するPDBエントリー: 3D3J
• 分子名称: Enhancer of mRNA-decapping protein 3 (2 entities in total)
• 機能のキーワード: hedc3, phosphoprotein, protein binding
• 由来する生物種: Homo sapiens (Human)
• 細胞内の位置: Cytoplasm, P-body: Q96F86
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 114348.53

構造登録者

Ling, S.H.M. (登録日: 2008-05-12, 公開日: 2008-08-26, 最終更新日: 2024-03-20)

主引用文献

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

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: 18678652
DOI: 10.1128/MCB.00761-08

実験手法

X-RAY DIFFRACTION (2.2 Å)