7DSD

CALHM1 close state with disordered CTH

7DSD の概要

• エントリーDOI: 10.2210/pdb7dsd/pdb
• EMDBエントリー: 30831
• 分子名称: Calcium homeostasis modulator 1, 2-acetamido-2-deoxy-beta-D-glucopyranose (2 entities in total)
• 機能のキーワード: close state, membrane protein
• 由来する生物種: Danio rerio (Zebrafish)
• タンパク質・核酸の鎖数: 7
• 化学式量合計: 280156.36

構造登録者

Ren, Y.,Yang, X.,Shen, Y.Q. (登録日: 2020-12-30, 公開日: 2022-01-05, 最終更新日: 2024-10-23)

主引用文献

Ren, Y.,Li, Y.,Wang, Y.,Wen, T.,Lu, X.,Chang, S.,Zhang, X.,Shen, Y.,Yang, X.
Cryo-EM structure of the heptameric calcium homeostasis modulator 1 channel.
J.Biol.Chem., 298:101838-101838, 2022

PubMed Abstract: Calcium homeostasis modulator 1 (CALHM1) is a voltage- and Ca-gated ATP channel that plays an important role in neuronal signaling. However, as the previously reported CALHM structures are all in the ATP-conducting state, the gating mechanism of ATP permeation is still elusive. Here, we report cryo-EM reconstructions of two Danio rerio CALHM1 heptamers with ordered or flexible long C-terminal helices at resolutions of 3.2 Å and 2.9 Å, respectively, and one D. rerio CALHM1 octamer with flexible long C-terminal helices at a resolution of 3.5 Å. Structural analysis shows that the heptameric CALHM1s are in an ATP-nonconducting state with a central pore diameter of approximately 6.6 Å. Compared with those inside the octameric CALHM1, the N-helix inside the heptameric CALHM1 is in the "down" position to avoid steric clashing with the adjacent TM1 helix. Molecular dynamics simulations show that as the N-helix moves from the "down" position to the "up" position, the pore size of ATP molecule permeation increases significantly. Our results provide important information for elucidating the mechanism of ATP molecule permeation in the CALHM1 channel.

PubMed: 35339491
DOI: 10.1016/j.jbc.2022.101838

実験手法

ELECTRON MICROSCOPY (2.9 Å)