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7TDH

Rabbit RyR1 with AMP-PCP and high Ca2+ embedded in nanodisc in open conformation

これはPDB形式変換不可エントリーです。
7TDH の概要
エントリーDOI10.2210/pdb7tdh/pdb
関連するPDBエントリー7K0T 7TDG 7TDI 7TDJ 7TDK
EMDBエントリー25829 25833
分子名称Ryanodine receptor 1,Ryanodine receptor 1,RyR1, ZINC ION, CALCIUM ION, ... (4 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: 2024-02-28)
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
Cited by
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
主引用文献が同じPDBエントリー
実験手法
ELECTRON MICROSCOPY (4 Å)
構造検証レポート
Validation report summary of 7tdh
検証レポート(詳細版)ダウンロードをダウンロード

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件を2025-12-31に公開中

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