5GKY

Structure of RyR1 in a closed state (C1 conformer)

これはPDB形式変換不可エントリーです。

5GKY の概要

• エントリーDOI: 10.2210/pdb5gky/pdb
• 関連するPDBエントリー: 3J8H 5GKZ 5GL0 5GL1
• EMDBエントリー: 9518
• 分子名称: Ryanodine receptor 1, Peptidyl-prolyl cis-trans isomerase FKBP1A, ZINC ION (3 entities in total)
• 機能のキーワード: channel, membrane protein, transport protein-isomerase complex, transport protein/isomerase
• 由来する生物種: Oryctolagus cuniculus (Rabbit); 詳細
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 2311766.96

構造登録者

Bai, X.C.,Yan, Z.,Wu, J.P.,Yan, N. (登録日: 2016-07-07, 公開日: 2016-08-24, 最終更新日: 2024-03-27)

主引用文献

Bai, X.C.,Yan, Z.,Wu, J.P.,Li, Z.Q.,Yan, N.
The Central domain of RyR1 is the transducer for long-range allosteric gating of channel opening
Cell Res., 26:995-1006, 2016

PubMed Abstract: The ryanodine receptors (RyRs) are intracellular calcium channels responsible for rapid release of Ca(2+) from the sarcoplasmic/endoplasmic reticulum (SR/ER) to the cytoplasm, which is essential for the excitation-contraction (E-C) coupling of cardiac and skeletal muscles. The near-atomic resolution structure of closed RyR1 revealed the molecular details of this colossal channel, while the long-range allosteric gating mechanism awaits elucidation. Here, we report the cryo-EM structures of rabbit RyR1 in three closed conformations at about 4 Å resolution and an open state at 5.7 Å. Comparison of the closed RyR1 structures shows a breathing motion of the cytoplasmic platform, while the channel domain and its contiguous Central domain remain nearly unchanged. Comparison of the open and closed structures shows a dilation of the S6 tetrahelical bundle at the cytoplasmic gate that leads to channel opening. During the pore opening, the cytoplasmic "O-ring" motif of the channel domain and the U-motif of the Central domain exhibit coupled motion, while the Central domain undergoes domain-wise displacement. These structural analyses provide important insight into the E-C coupling in skeletal muscles and identify the Central domain as the transducer that couples the conformational changes of the cytoplasmic platform to the gating of the central pore.

PubMed: 27468892
DOI: 10.1038/cr.2016.89

実験手法

ELECTRON MICROSCOPY (3.8 Å)