5OPW

Crystal structure of the GroEL mutant A109C

5OPW の概要

• エントリーDOI: 10.2210/pdb5opw/pdb
• 関連するPDBエントリー: 5OPX
• 分子名称: 60 kDa chaperonin (1 entity in total)
• 機能のキーワード: chaperonin, chaperone
• 由来する生物種: Escherichia coli (strain K12)
• 細胞内の位置: Cytoplasm : P0A6F5
• タンパク質・核酸の鎖数: 14
• 化学式量合計: 802095.92

構造登録者

Yan, X.,Shi, Q.,Bracher, A.,Milicic, G.,Singh, A.K.,Hartl, F.U.,Hayer-Hartl, M. (登録日: 2017-08-10, 公開日: 2018-01-10, 最終更新日: 2024-01-17)

主引用文献

Yan, X.,Shi, Q.,Bracher, A.,Milicic, G.,Singh, A.K.,Hartl, F.U.,Hayer-Hartl, M.
GroEL Ring Separation and Exchange in the Chaperonin Reaction.
Cell, 172:605-617.e11, 2018

PubMed Abstract: The bacterial chaperonin GroEL and its cofactor, GroES, form a nano-cage for a single molecule of substrate protein (SP) to fold in isolation. GroEL and GroES undergo an ATP-regulated interaction cycle to close and open the folding cage. GroEL consists of two heptameric rings stacked back to back. Here, we show that GroEL undergoes transient ring separation, resulting in ring exchange between complexes. Ring separation occurs upon ATP-binding to the trans ring of the asymmetric GroEL:7ADP:GroES complex in the presence or absence of SP and is a consequence of inter-ring negative allostery. We find that a GroEL mutant unable to perform ring separation is folding active but populates symmetric GroEL:GroES complexes, where both GroEL rings function simultaneously rather than sequentially. As a consequence, SP binding and release from the folding chamber is inefficient, and E. coli growth is impaired. We suggest that transient ring separation is an integral part of the chaperonin mechanism.

PubMed: 29336887
DOI: 10.1016/j.cell.2017.12.010

実験手法

X-RAY DIFFRACTION (3.19 Å)