5M2N

Crystal Structure of Elongator subunit Elp2

5M2N の概要

• エントリーDOI: 10.2210/pdb5m2n/pdb
• 関連するPDBエントリー: 4XFV
• 分子名称: Elongator complex protein 2 (2 entities in total)
• 機能のキーワード: elongator, trna modifcation, elp2, wd40, rna binding protein
• 由来する生物種: Saccharomyces cerevisiae (Baker's yeast)
• 細胞内の位置: Cytoplasm: P42935
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 90129.08

構造登録者

Glatt, S.,Mueller, C.W. (登録日: 2016-10-13, 公開日: 2016-12-28, 最終更新日: 2024-11-13)

主引用文献

Dauden, M.I.,Kosinski, J.,Kolaj-Robin, O.,Desfosses, A.,Ori, A.,Faux, C.,Hoffmann, N.A.,Onuma, O.F.,Breunig, K.D.,Beck, M.,Sachse, C.,Seraphin, B.,Glatt, S.,Muller, C.W.
Architecture of the yeast Elongator complex.
EMBO Rep., 18:264-279, 2017

PubMed Abstract: The highly conserved eukaryotic Elongator complex performs specific chemical modifications on wobble base uridines of tRNAs, which are essential for proteome stability and homeostasis. The complex is formed by six individual subunits (Elp1-6) that are all equally important for its tRNA modification activity. However, its overall architecture and the detailed reaction mechanism remain elusive. Here, we report the structures of the fully assembled yeast Elongator and the Elp123 sub-complex solved by an integrative structure determination approach showing that two copies of the Elp1, Elp2, and Elp3 subunits form a two-lobed scaffold, which binds Elp456 asymmetrically. Our topological models are consistent with previous studies on individual subunits and further validated by complementary biochemical analyses. Our study provides a structural framework on how the tRNA modification activity is carried out by Elongator.

PubMed: 27974378
DOI: 10.15252/embr.201643353

実験手法

X-RAY DIFFRACTION (2.812 Å)