7TDJ

Rabbit RyR1 with AMP-PCP and high Ca2+ embedded in nanodisc in closed-inactivated conformation class 1(Dataset-A)

これはPDB形式変換不可エントリーです。

7TDJ の概要

• エントリーDOI: 10.2210/pdb7tdj/pdb
• 関連するPDBエントリー: 7K0T 7TDG 7TDH 7TDI 7TDK
• EMDBエントリー: 25831 25833
• 分子名称: Ryanodine receptor 1,Ryanodine receptor 1,RyR1, PHOSPHOMETHYLPHOSPHONIC ACID ADENYLATE ESTER, ZINC ION, ... (5 entities in total)
• 機能のキーワード: ryanodine receptor, ryr1, intracellular calcium channel, ca2+, inactivation, excitation-contraction coupling, transport protein
• 由来する生物種: Oryctolagus cuniculus (rabbit); 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 2137256.09

構造登録者

Nayak, A.R.,Samso, M. (登録日: 2021-12-31, 公開日: 2022-03-09, 最終更新日: 2024-10-30)

主引用文献

Nayak, A.R.,Samso, M.
Ca 2+ -inactivation of the mammalian ryanodine receptor type 1 in a lipidic environment revealed by cryo-EM.
Elife, 11:-, 2022

PubMed Abstract: Activation of the intracellular Ca channel ryanodine receptor (RyR) triggers a cytosolic Ca surge, while elevated cytosolic Ca inhibits the channel in a negative feedback mechanism. Cryogenic electron microscopy of rabbit RyR1 embedded in nanodiscs under partially inactivating Ca conditions revealed an open and a closed-inactivated conformation. Ca binding to the high-affinity site engages the central and C-terminal domains into a block, which pries the S6 four-helix bundle open. Further rotation of this block pushes S6 toward the central axis, closing (inactivating) the channel. Main characteristics of the Ca-inactivated conformation are downward conformation of the cytoplasmic assembly and tightly knit subunit interface contributed by a fully occupied Ca activation site, two inter-subunit resolved lipids, and two salt bridges between the EF hand domain and the S2-S3 loop validated by disease-causing mutations. The structural insight illustrates the prior Ca activation prerequisite for Ca inactivation and provides for a seamless transition from inactivated to closed conformations.

PubMed: 35257661
DOI: 10.7554/eLife.75568

実験手法

ELECTRON MICROSCOPY (3.7 Å)