3VWA

Crystal structure of Cex1p

3VWA の概要

• エントリーDOI: 10.2210/pdb3vwa/pdb
• 分子名称: Cytoplasmic export protein 1 (2 entities in total)
• 機能のキーワード: trna, nuclear export, heat repeat, kinase like domain, hydrolase
• 由来する生物種: Saccharomyces cerevisiae (yeast)
• 細胞内の位置: Cytoplasm: Q12453
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 126627.20

構造登録者

Nozawa, K.,Ishitani, R.,Nureki, O. (登録日: 2012-08-13, 公開日: 2013-06-05, 最終更新日: 2024-11-06)

主引用文献

Nozawa, K.,Ishitani, R.,Yoshihisa, T.,Sato, M.,Arisaka, F.,Kanamaru, S.,Dohmae, N.,Mangroo, D.,Senger, B.,Becker, H.D.,Nureki, O.
Crystal structure of Cex1p reveals the mechanism of tRNA trafficking between nucleus and cytoplasm
Nucleic Acids Res., 41:3901-3914, 2013

PubMed Abstract: In all eukaryotes, transcribed precursor tRNAs are maturated by processing and modification processes in nucleus and are transported to the cytoplasm. The cytoplasmic export protein (Cex1p) captures mature tRNAs from the nuclear export receptor (Los1p) on the cytoplasmic side of the nuclear pore complex, and it delivers them to eukaryotic elongation factor 1α. This conserved Cex1p function is essential for the quality control of mature tRNAs to ensure accurate translation. However, the structural basis of how Cex1p recognizes tRNAs and shuttles them to the translational apparatus remains unclear. Here, we solved the 2.2 Å resolution crystal structure of Saccharomyces cerevisiae Cex1p with C-terminal 197 disordered residues truncated. Cex1p adopts an elongated architecture, consisting of N-terminal kinase-like and a C-terminal α-helical HEAT repeat domains. Structure-based biochemical analyses suggested that Cex1p binds tRNAs on its inner side, using the positively charged HEAT repeat surface and the C-terminal disordered region. The N-terminal kinase-like domain acts as a scaffold to interact with the Ran-exportin (Los1p·Gsp1p) machinery. These results provide the structural basis of Los1p·Gsp1p·Cex1p·tRNA complex formation, thus clarifying the dynamic mechanism of tRNA shuttling from exportin to the translational apparatus.

PubMed: 23396276
DOI: 10.1093/nar/gkt010

実験手法

X-RAY DIFFRACTION (2.2 Å)