5OWJ

The dynamic dimer structure of the chaperone Trigger Factor (conformer 2)

5OWJ の概要

• エントリーDOI: 10.2210/pdb5owj/pdb
• 関連するPDBエントリー: 5OWI
• NMR情報: BMRB: 27242
• 分子名称: Trigger factor (1 entity in total)
• 機能のキーワード: chaperone, dimer
• 由来する生物種: Escherichia coli
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 96511.14

構造登録者

Morgado, L.,Burmann, B.M.,Sharpe, T.,Mazur, A.,Hiller, S. (登録日: 2017-09-01, 公開日: 2017-11-29, 最終更新日: 2024-05-15)

主引用文献

Morgado, L.,Burmann, B.M.,Sharpe, T.,Mazur, A.,Hiller, S.
The dynamic dimer structure of the chaperone Trigger Factor.
Nat Commun, 8:1992-1992, 2017

PubMed Abstract: The chaperone Trigger Factor (TF) from Escherichia coli forms a dimer at cellular concentrations. While the monomer structure of TF is well known, the spatial arrangement of this dimeric chaperone storage form has remained unclear. Here, we determine its structure by a combination of high-resolution NMR spectroscopy and biophysical methods. TF forms a symmetric head-to-tail dimer, where the ribosome binding domain is in contact with the substrate binding domain, while the peptidyl-prolyl isomerase domain contributes only slightly to the dimer affinity. The dimer structure is highly dynamic, with the two ribosome binding domains populating a conformational ensemble in the center. These dynamics result from intermolecular in trans interactions of the TF client-binding site with the ribosome binding domain, which is conformationally frustrated in the absence of the ribosome. The avidity in the dimer structure explains how the dimeric state of TF can be monomerized also by weakly interacting clients.

PubMed: 29222465
DOI: 10.1038/s41467-017-02196-7

実験手法

SOLUTION NMR