3WXM

Crystal structure of archaeal Pelota and GTP-bound EF1 alpha complex

「3AGJ」から置き換えられました

3WXM の概要

• エントリーDOI: 10.2210/pdb3wxm/pdb
• 分子名称: Elongation factor 1-alpha, Protein pelota homolog, GUANOSINE-5'-TRIPHOSPHATE, ... (5 entities in total)
• 機能のキーワード: mrna surveillance, ribosome, translation-hydrolase complex, translation/hydrolase
• 由来する生物種: Aeropyrum pernix K1; 詳細
• 細胞内の位置: Cytoplasm (By similarity): Q9YAV0; Cytoplasm (Potential): Q9YAZ5
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 366722.58

構造登録者

Kobayashi, K.,Ishitani, R.,Nureki, O. (登録日: 2014-08-04, 公開日: 2014-09-03, 最終更新日: 2024-03-20)

主引用文献

Kobayashi, K.,Kikuno, I.,Kuroha, K.,Saito, K.,Ito, K.,Ishitani, R.,Inada, T.,Nureki, O.
Structural basis for mRNA surveillance by archaeal Pelota and GTP-bound EF1 alpha complex
Proc.Natl.Acad.Sci.USA, 107:17575-17579, 2010

PubMed Abstract: No-go decay and nonstop decay are mRNA surveillance pathways that detect translational stalling and degrade the underlying mRNA, allowing the correct translation of the genetic code. In eukaryotes, the protein complex of Pelota (yeast Dom34) and Hbs1 translational GTPase recognizes the stalled ribosome containing the defective mRNA. Recently, we found that archaeal Pelota (aPelota) associates with archaeal elongation factor 1α (aEF1α) to act in the mRNA surveillance pathway, which accounts for the lack of an Hbs1 ortholog in archaea. Here we present the complex structure of aPelota and GTP-bound aEF1α determined at 2.3-Å resolution. The structure reveals how GTP-bound aEF1α recognizes aPelota and how aPelota in turn stabilizes the GTP form of aEF1α. Combined with the functional analysis in yeast, the present results provide structural insights into the molecular interaction between eukaryotic Pelota and Hbs1. Strikingly, the aPelota·aEF1α complex structurally resembles the tRNA·EF-Tu complex bound to the ribosome. Our findings suggest that the molecular mimicry of tRNA in the distorted "A/T state" conformation by Pelota enables the complex to efficiently detect and enter the empty A site of the stalled ribosome.

PubMed: 20876129
DOI: 10.1073/pnas.1009598107

実験手法

X-RAY DIFFRACTION (2.3 Å)