Conformational shift in the closed state of GroEL induced by ATP-binding triggers a transition to the open state

Yuka Suzuki, Kei Yura*

*この研究の対応する著者

研究成果: Article査読

4 被引用数 (Scopus)

抄録

We investigated the effect of ATP binding to GroEL and elucidated a role of ATP in the conformational change of GroEL. GroEL is a tetradecamer chaperonin that helps protein folding by undergoing a conformational change from a closed state to an open state. This conformational change requires ATP, but does not require the hydrolysis of the ATP. The following three types of conformations are crystalized and the atomic coordinates are available; closed state without ATP, closed state with ATP and open state with ADP. We conducted simulations of the conformational change using Elastic Network Model from the closed state without ATP targeting at the open state, and from the closed state with ATP targeting at the open state. The simulations emphasizing the lowest normal mode showed that the one started with the closed state with ATP, rather than the one without ATP, reached a conformation closer to the open state. This difference was mainly caused by the changes in the positions of residues in the initial structure rather than the changes in “connectivity” of residues within the subunit. Our results suggest that ATP should behave as an insulator to induce confor mation population shift in the closed state to the conformation that has a pathway leading to the open state.

本文言語English
ページ(範囲)127-134
ページ数8
ジャーナルBiophysics and physicobiology
13
DOI
出版ステータスPublished - 2016
外部発表はい

ASJC Scopus subject areas

  • 生物理学
  • 生化学
  • 分子生物学
  • 生理学
  • 生化学、遺伝学、分子生物学(その他)

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