- EMDB-21143: Cryo-EM structure of octameric chicken CALHM1 -
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基本情報
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データベース: EMDB / ID: EMD-21143
タイトル
Cryo-EM structure of octameric chicken CALHM1
マップデータ
sharpened map of chicken calcium homeostasis modulator protein 1
試料
複合体: Octameric chicken CALHM1 in EDTA
タンパク質・ペプチド: Green fluorescent protein,CALHM1 chimera
機能・相同性
機能・相同性情報
voltage-gated monoatomic ion channel activity / calcium-activated cation channel activity / monoatomic cation channel activity / bioluminescence / generation of precursor metabolites and energy / plasma membrane 類似検索 - 分子機能
Calcium homeostasis modulator protein 1 / Calcium homeostasis modulator family / Calcium homeostasis modulator / Green fluorescent protein, GFP / Green fluorescent protein-related / Green fluorescent protein / Green fluorescent protein 類似検索 - ドメイン・相同性
Calcium homeostasis modulator 1 / Green fluorescent protein 類似検索 - 構成要素
National Institutes of Health/National Institute of Neurological Disorders and Stroke (NIH/NINDS)
米国
National Institutes of Health/National Institute of Mental Health (NIH/NIMH)
引用
ジャーナル: Nat Struct Mol Biol / 年: 2020 タイトル: Structure and assembly of calcium homeostasis modulator proteins. 著者: Johanna L Syrjanen / Kevin Michalski / Tsung-Han Chou / Timothy Grant / Shanlin Rao / Noriko Simorowski / Stephen J Tucker / Nikolaus Grigorieff / Hiro Furukawa / 要旨: The biological membranes of many cell types contain large-pore channels through which a wide variety of ions and metabolites permeate. Examples include connexin, innexin and pannexin, which form gap ...The biological membranes of many cell types contain large-pore channels through which a wide variety of ions and metabolites permeate. Examples include connexin, innexin and pannexin, which form gap junctions and/or bona fide cell surface channels. The most recently identified large-pore channels are the calcium homeostasis modulators (CALHMs), through which ions and ATP permeate in a voltage-dependent manner to control neuronal excitability, taste signaling and pathologies of depression and Alzheimer's disease. Despite such critical biological roles, the structures and patterns of their oligomeric assembly remain unclear. Here, we reveal the structures of two CALHMs, chicken CALHM1 and human CALHM2, by single-particle cryo-electron microscopy (cryo-EM), which show novel assembly of the four transmembrane helices into channels of octamers and undecamers, respectively. Furthermore, molecular dynamics simulations suggest that lipids can favorably assemble into a bilayer within the larger CALHM2 pore, but not within CALHM1, demonstrating the potential correlation between pore size, lipid accommodation and channel activity.
EMPIAR-10485 (タイトル: Chicken CALHM1, 1 mM EDTA / Data size: 2.4 TB Data #1: Unaligned movies (.tif) for chicken CALHM1 in nanodisc [micrographs - multiframe])