4C92

Crystal structure of the yeast Lsm1-7 complex

4C92 の概要

• エントリーDOI: 10.2210/pdb4c92/pdb
• 関連するPDBエントリー: 4C8Q
• 分子名称: SM-LIKE PROTEIN LSM1, U6 SNRNA-ASSOCIATED SM-LIKE PROTEIN LSM2, U6 SNRNA-ASSOCIATED SM-LIKE PROTEIN LSM3, ... (8 entities in total)
• 機能のキーワード: transcription, lsm1-7, decapping activators, mrna degradation
• 由来する生物種: SACCHAROMYCES CEREVISIAE (BAKER'S YEAST); 詳細
• 細胞内の位置: Nucleus: P47017 P38203 P57743 P40070 P40089 P53905; Cytoplasm: Q06406
• タンパク質・核酸の鎖数: 7
• 化学式量合計: 85445.86

構造登録者

Sharif, H.,Conti, E. (登録日: 2013-10-02, 公開日: 2013-10-16, 最終更新日: 2023-12-20)

主引用文献

Sharif, H.,Conti, E.
Architecture of the Lsm1-7-Pat1 Complex: A Conserved Assembly in Eukaryotic Mrna Turnover
Cell Rep., 5:283-, 2013

PubMed Abstract: The decay of mRNAs is a key step in eukaryotic gene expression. The cytoplasmic Lsm1-7-Pat1 complex is a conserved component of the 5'-to-3' mRNA decay pathway, linking deadenylation to decapping. Lsm1-7 is similar to the nuclear Sm complexes that bind oligo-uridine tracts in snRNAs. The 2.3 Å resolution structure of S. cerevisiae Lsm1-7 shows the presence of a heptameric ring with Lsm1-2-3-6-5-7-4 topology. A distinct structural feature of the cytoplasmic Lsm ring is the C-terminal extension of Lsm1, which plugs the exit site of the central channel and approaches the RNA binding pockets. The 3.7 Å resolution structure of Lsm1-7 bound to the C-terminal domain of Pat1 reveals that Pat1 recognition is not mediated by the distinguishing cytoplasmic subunit, Lsm1, but by Lsm2 and Lsm3. These results show how the auxiliary domains and the canonical Sm folds of the Lsm1-7 complex are organized in order to mediate and modulate macromolecular interactions.

PubMed: 24139796
DOI: 10.1016/J.CELREP.2013.10.004

実験手法

X-RAY DIFFRACTION (2.299 Å)