1I5L

CRYSTAL STRUCTURE OF AN SM-LIKE PROTEIN (AF-SM1) FROM ARCHAEOGLOBUS FULGIDUS COMPLEXED WITH SHORT POLY-U RNA

1I5L の概要

• エントリーDOI: 10.2210/pdb1i5l/pdb
• 関連するPDBエントリー: 1B34 1D3B 1I4K
• 分子名称: 5'-R(*UP*UP*U)-3', PUTATIVE SNRNP SM-LIKE PROTEIN AF-SM1, URIDINE, ... (4 entities in total)
• 機能のキーワード: snrnp, sm, core snrnp domain, rna binding protein, single-stranded rna binding protein, rna binding protein-rna complex, rna binding protein/rna
• 由来する生物種: Archaeoglobus fulgidus
• タンパク質・核酸の鎖数: 16
• 化学式量合計: 120207.81

構造登録者

Toro, I.,Thore, S.,Mayer, C.,Basquin, J.,Seraphin, B.,Suck, D. (登録日: 2001-02-28, 公開日: 2001-08-28, 最終更新日: 2024-04-03)

主引用文献

Toro, I.,Thore, S.,Mayer, C.,Basquin, J.,Seraphin, B.,Suck, D.
RNA binding in an Sm core domain: X-ray structure and functional analysis of an archaeal Sm protein complex.
EMBO J., 20:2293-2303, 2001

PubMed Abstract: Eukaryotic Sm and Sm-like proteins associate with RNA to form the core domain of ribonucleoprotein particles involved in pre-mRNA splicing and other processes. Recently, putative Sm proteins of unknown function have been identified in Archaea. We show by immunoprecipitation experiments that the two Sm proteins present in Archaeoglobus fulgidus (AF-Sm1 and AF-Sm2) associate with RNase P RNA in vivo, suggesting a role in tRNA processing. The AF-Sm1 protein also interacts specifically with oligouridylate in vitro. We have solved the crystal structures of this protein and a complex with RNA. AF-Sm1 forms a seven-membered ring, with the RNA interacting inside the central cavity on one face of the doughnut-shaped complex. The bases are bound via stacking and specific hydrogen bonding contacts in pockets lined by residues highly conserved in archaeal and eukaryotic Sm proteins, while the phosphates remain solvent accessible. A comparison with the structures of human Sm protein dimers reveals closely related monomer folds and intersubunit contacts, indicating that the architecture of the Sm core domain and RNA binding have been conserved during evolution.

PubMed: 11331594
DOI: 10.1093/emboj/20.9.2293

実験手法

X-RAY DIFFRACTION (2.75 Å)