1RYM

Structure of the Group II Intron Splicing Factor CRS2

1RYM の概要

• エントリーDOI: 10.2210/pdb1rym/pdb
• 関連するPDBエントリー: 1RYB 1RYN
• 分子名称: protein CRS2 (2 entities in total)
• 機能のキーワード: alpha-beta, translation
• 由来する生物種: Zea mays
• 細胞内の位置: Plastid, chloroplast stroma: Q9M5P4
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 23655.94

構造登録者

Ostheimer, G.J.,Barkan, A.,Matthews, B.W. (登録日: 2003-12-22, 公開日: 2004-01-06, 最終更新日: 2024-04-03)

主引用文献

Ostheimer, G.J.,Hadjivasiliou, H.,Kloer, D.P.,Barkan, A.,Matthews, B.W.
Structural analysis of the group II intron splicing factor CRS2 yields insights into its protein and RNA interaction surfaces
J.Mol.Biol., 345:51-68, 2005

PubMed Abstract: Chloroplast RNA splicing 2 (CRS2) is a nuclear-encoded protein required for the splicing of nine group II introns in maize chloroplasts. CRS2 functions in the context of splicing complexes that include one of two CRS2-associated factors (CAF1 and CAF2). The CRS2-CAF1 and CRS2-CAF2 complexes are required for the splicing of different subsets of CRS2-dependent introns, and they bind tightly and specifically to their genetically defined intron targets in vivo. The CRS2 amino acid sequence is closely related to those of bacterial peptidyl-tRNA hydrolases (PTHs). To identify the structural differences between CRS2 and bacterial PTHs responsible for CRS2's gains of CAF binding and intron splicing functions, we determined the structure of CRS2 by X-ray crystallography. The fold of CRS2 is the same as that of Escherichia coli PTH, but CRS2 has two surfaces that differ from the corresponding surfaces in PTH. One of these is more hydrophobic in CRS2 than in PTH. Site-directed mutagenesis of this surface blocked CRS2-CAF complex formation, indicating that it is the CAF binding site. The CRS2 surface corresponding to the putative tRNA binding face of PTH is considerably more basic than in PTH, suggesting that CRS2 interacts with group II intron substrates via this surface. Both the sequence and the structural context of the amino acid residues essential for peptidyl-tRNA hydrolase activity are conserved in CRS2, yet expression of CRS2 is incapable of rescuing a pth(ts)E.coli strain.

PubMed: 15567410
DOI: 10.1016/j.jmb.2004.10.032

実験手法

X-RAY DIFFRACTION (1.8 Å)