2AAR

Structure of trigger factor binding domain in biologically homologous complex with eubacterial ribosome.

2AAR の概要

• エントリーDOI: 10.2210/pdb2aar/pdb
• 関連するPDBエントリー: 1NKW
• 分子名称: 23S ribosomal RNA, 50S ribosomal protein L23, 50S ribosomal protein L29, ... (4 entities in total)
• 機能のキーワード: trigger factor, 50s, ribosome, cheperone, tunnel
• 由来する生物種: Deinococcus radiodurans; 詳細
• 細胞内の位置: Cytoplasm: Q9RT21
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 964308.30

構造登録者

Baram, D.,Pyetan, E.,Sittner, A.,Auerbach-Nevo, T.,Bashan, A.,Yonath, A. (登録日: 2005-07-14, 公開日: 2005-08-23, 最終更新日: 2023-08-23)

主引用文献

Baram, D.,Pyetan, E.,Sittner, A.,Auerbach-Nevo, T.,Bashan, A.,Yonath, A.
Structure of trigger factor binding domain in biologically homologous complex with eubacterial ribosome reveals its chaperone action
Proc.Natl.Acad.Sci.Usa, 102:12017-12022, 2005

PubMed Abstract: Trigger factor (TF), the first chaperone in eubacteria to encounter the emerging nascent chain, binds to the large ribosomal subunit in the vicinity of the protein exit tunnel opening and forms a sheltered folding space. Here, we present the 3.5-A crystal structure of the physiological complex of the large ribosomal subunit from the eubacterium Deinococcus radiodurans with the N-terminal domain of TF (TFa) from the same organism. For anchoring, TFa exploits a small ribosomal surface area in the vicinity of proteins L23 and L29, by using its "signature motif" as well as additional structural elements. The molecular details of TFa interactions reveal that L23 is essential for the association of TF with the ribosome and may serve as a channel of communication with the nascent chain progressing in the tunnel. L29 appears to induce a conformational change in TFa, which results in the exposure of TFa hydrophobic patches to the opening of the ribosomal exit tunnel, thus increasing its affinity for hydrophobic segments of the emerging nascent polypeptide. This observation implies that, in addition to creating a protected folding space for the emerging nascent chain, TF association with the ribosome prevents aggregation by providing a competing hydrophobic environment and may be critical for attaining the functional conformation necessary for chaperone activity.

PubMed: 16091460
DOI: 10.1073/pnas.0505581102

実験手法

X-RAY DIFFRACTION (3.5 Å)