8X4E

Cryo-EM structure of Ryanodine receptor 1 (TM helix S0, 5 mM Ca2+)

これはPDB形式変換不可エントリーです。

8X4E の概要

• エントリーDOI: 10.2210/pdb8x4e/pdb
• EMDBエントリー: 38048
• 分子名称: Ryanodine receptor 1, ZINC ION, CALCIUM ION (3 entities in total)
• 機能のキーワード: ryanodine receptor, calcium release channel, membrane protein
• 由来する生物種: Oryctolagus cuniculus (rabbit)
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 2264056.45

構造登録者

Chen, Q.,Hu, H. (登録日: 2023-11-15, 公開日: 2025-03-05, 最終更新日: 2025-03-12)

主引用文献

Wei, R.,Chen, Q.,Zhang, L.,Liu, C.,Liu, C.,Yin, C.C.,Hu, H.
Structural insights into transmembrane helix S0 facilitated RyR1 channel gating by Ca 2+ /ATP.
Nat Commun, 16:1936-1936, 2025

PubMed Abstract: The type-1 ryanodine receptor (RyR1) is an intracellular calcium release channel for skeletal muscle excitation-contraction coupling. Previous structural studies showed that the RyR1 activity is modulated by the exogenous regulators including caffeine, ryanodine, PCB-95 and diamide. An additional transmembrane helix, located adjacent to S1 and S4, has been observed in some structures, although its function remains unclear. Here, we report that using a mild purification procedure, this helix is co-purified with RyR1 and is designated as S0. When RyR1 is coupled with S0, it can be activated by Ca to an open state; however when decoupled from S0, it remains in primed state. S0 regulates the channel conformation by directly affecting the TM domain via the pVSD-S0-S4/S5 linker coupling, which facilitates the dilation of S6. Our results demonstrate that S0 is an essential component of RyR1 and plays a key role in the physiological regulation of RyR1 channel gating.

PubMed: 39994184
DOI: 10.1038/s41467-025-57074-4

実験手法

ELECTRON MICROSCOPY (3.3 Å)