1OMS

Structure determination by MAD: E.coli Trigger Factor binding at the ribosomal exit tunnel.

1OMS の概要

• エントリーDOI: 10.2210/pdb1oms/pdb
• 分子名称: Trigger Factor, SULFATE ION, TETRAETHYLENE GLYCOL, ... (6 entities in total)
• 機能のキーワード: alpha-beta structure, isomerase
• 由来する生物種: Escherichia coli
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 42890.83

構造登録者

Kristensen, O.,Gajhede, M. (登録日: 2003-02-26, 公開日: 2003-12-16, 最終更新日: 2024-11-13)

主引用文献

Kristensen, O.,Gajhede, M.
Chaperone binding at the ribosomal exit tunnel.
Structure, 11:1547-1556, 2003

PubMed Abstract: The exit tunnel region of the ribosome is well established as a focal point for interaction between the components that guide the fate of nascent polypeptides. One of these, the chaperone trigger factor (TF), associates with the 50S ribosomal subunit through its N-terminal domain. Targeting of TF to ribosomes is crucial to achieve its remarkable efficiency in protein folding. A similar tight coupling to translation is found in signal recognition particle (SRP)-dependent protein translocation. Here, we report crystal structures of the E. coli TF ribosome binding domain. TF is structurally related to the Hsp33 chaperone but has a prominent ribosome anchor located as a tip of the molecule. This tip includes the previously established unique TF signature motif. Comparison reveals that this feature is not found in SRP structures. We identify a conserved helical kink as a hallmark of the TF structure that is most likely critical to ensure ribosome association.

PubMed: 14656439
DOI: 10.1016/j.str.2003.11.003

実験手法

X-RAY DIFFRACTION (2.3 Å)