4V4Y

Crystal structure of the 70S Thermus thermophilus ribosome with translocated and rotated Shine-Dalgarno Duplex.

これはPDB形式変換不可エントリーです。

4V4Y の概要

• エントリーDOI: 10.2210/pdb4v4y/pdb
• 関連するPDBエントリー: 2HGQ
• 分子名称: 16S ribosomal RNA, 30S ribosomal protein S8, 30S ribosomal protein S9, ... (55 entities in total)
• 機能のキーワード: ribosome, shine-dalgarno, post-initiation
• 由来する生物種: Thermus thermophilus; 詳細
• タンパク質・核酸の鎖数: 57
• 化学式量合計: 2287270.81

構造登録者

Jenner, L.,Yusupova, G.,Rees, B.,Moras, D.,Yusupov, M. (登録日: 2006-06-27, 公開日: 2014-07-09, 最終更新日: 2017-11-22)

主引用文献

Yusupova, G.,Jenner, L.,Rees, B.,Moras, D.,Yusupov, M.
Structural basis for messenger RNA movement on the ribosome.
Nature, 444:391-394, 2006

PubMed Abstract: Translation initiation is a major determinant of the overall expression level of a gene. The translation of functionally active protein requires the messenger RNA to be positioned on the ribosome such that the start/initiation codon will be read first and in the correct frame. Little is known about the molecular basis for the interaction of mRNA with the ribosome at different states of translation. Recent crystal structures of the ribosomal subunits, the empty 70S ribosome and the 70S ribosome containing functional ligands have provided information about the general organization of the ribosome and its functional centres. Here we compare the X-ray structures of eight ribosome complexes modelling the translation initiation, post-initiation and elongation states. In the initiation and post-initiation complexes, the presence of the Shine-Dalgarno (SD) duplex causes strong anchoring of the 5'-end of mRNA onto the platform of the 30S subunit, with numerous interactions between mRNA and the ribosome. Conversely, the 5' end of the 'elongator' mRNA lacking SD interactions is flexible, suggesting a different exit path for mRNA during elongation. After the initiation of translation, but while an SD interaction is still present, mRNA moves in the 3'-->5' direction with simultaneous clockwise rotation and lengthening of the SD duplex, bringing it into contact with ribosomal protein S2.

PubMed: 17051149
DOI: 10.1038/nature05281

実験手法

X-RAY DIFFRACTION (5.5 Å)