2PJP

Structure of the mRNA-binding domain of elongation factor SelB from E.coli in complex with SECIS RNA

2PJP の概要

• エントリーDOI: 10.2210/pdb2pjp/pdb
• 分子名称: SECIS RNA, Selenocysteine-specific elongation factor, MAGNESIUM ION, ... (7 entities in total)
• 機能のキーワード: selb, protein-rna complex, elongation factor, secis, winged-helix, bulge, translation-rna complex, translation/rna
• 由来する生物種: Escherichia coli; 詳細
• 細胞内の位置: Cytoplasm: 2PJP
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 22282.82

構造登録者

Soler, N.,Fourmy, D.,Yoshizawa, S. (登録日: 2007-04-16, 公開日: 2007-10-30, 最終更新日: 2023-08-30)

主引用文献

Soler, N.,Fourmy, D.,Yoshizawa, S.
Structural insight into a molecular switch in tandem winged-helix motifs from elongation factor SelB.
J.Mol.Biol., 370:728-741, 2007

PubMed Abstract: Elongation factor SelB is responsible for co-translational incorporation of selenocysteine (Sec) into proteins. The UGA stop codon is recoded as a Sec codon in the presence of a downstream mRNA hairpin. In prokaryotes, in addition to the EF-Tu-like N-terminal domains, a C-terminal extension containing four tandem winged-helix motifs (WH1-4) recognizes the mRNA hairpin. The 2.3-A resolution crystal structure of the Escherichia coli WH3/4 domains bound to mRNA with mutagenesis data reveal that the two WH motifs use the same structural elements to bind RNA. The structure together with the 2.6-A resolution structure of the WH1-4 domains from Moorella thermoacetica bound to RNA revealed that a salt bridge connecting WH2 to WH3 modules is disrupted upon mRNA binding. The results provide a structural basis for the molecular switch that may allow communication between tRNA and mRNA binding sites and illustrate how RNA acts as an activator of the switch. The structures show that tandem WH motifs not only provide an excellent scaffold for RNA binding but can also have an active role in the function of protein-RNA complexes.

PubMed: 17537456
DOI: 10.1016/j.jmb.2007.05.001

実験手法

X-RAY DIFFRACTION (2.3 Å)