1H64

CRYSTAL STRUCTURE OF THE SM-RELATED PROTEIN OF P. ABYSSI: THE BIOLOGICAL UNIT IS A HEPTAMER

1H64 の概要

• エントリーDOI: 10.2210/pdb1h64/pdb
• 分子名称: SNRNP SM-LIKE PROTEIN (2 entities in total)
• 機能のキーワード: sm-like protein, sm fold, spliceosome, snrnp core
• 由来する生物種: PYROCOCCUS ABYSSI
• タンパク質・核酸の鎖数: 28
• 化学式量合計: 238053.17

構造登録者

Mayer, C.,Weeks, S.,Suck, D. (登録日: 2001-06-05, 公開日: 2002-12-19, 最終更新日: 2024-05-01)

主引用文献

Thore, S.,Mayer, C.,Sauter, C.,Weeks, S.,Suck, D.
Crystal Structures of the Pyrococcus Abyssi Sm Core and its Complex with RNA.Common Features of RNA Binding in Archaea and Eukarya
J.Biol.Chem., 278:1239-, 2003

PubMed Abstract: The Sm proteins are conserved in all three domains of life and are always associated with U-rich RNA sequences. Their proposed function is to mediate RNA-RNA interactions. We present here the crystal structures of Pyrococcus abyssi Sm protein (PA-Sm1) and its complex with a uridine heptamer. The overall structure of the protein complex, a heptameric ring with a central cavity, is similar to that proposed for the eukaryotic Sm core complex and found for other archaeal Sm proteins. RNA molecules bind to the protein at two different sites. They interact specifically inside the ring with three highly conserved residues, defining the uridine-binding pocket. In addition, nucleotides also interact on the surface formed by the N-terminal alpha-helix as well as a conserved aromatic residue in beta-strand 2 of the PA-Sm1 protein. The mutation of this conserved aromatic residue shows the importance of this second site for the discrimination between RNA sequences. Given the high structural homology between archaeal and eukaryotic Sm proteins, the PA-Sm1.RNA complex provides a model for how the small nuclear RNA contacts the Sm proteins in the Sm core. In addition, it suggests how Sm proteins might exert their function as modulators of RNA-RNA interactions.

PubMed: 12409299
DOI: 10.1074/JBC.M207685200

実験手法

X-RAY DIFFRACTION (1.9 Å)