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-Structure paper
タイトル | Cryo-EM structures of calcium homeostasis modulator channels in diverse oligomeric assemblies. |
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ジャーナル・号・ページ | Sci Adv, Vol. 6, Issue 29, Page eaba8105, Year 2020 |
掲載日 | 2020年7月17日 |
著者 | Kanae Demura / Tsukasa Kusakizako / Wataru Shihoya / Masahiro Hiraizumi / Kengo Nomura / Hiroto Shimada / Keitaro Yamashita / Tomohiro Nishizawa / Akiyuki Taruno / Osamu Nureki / |
PubMed 要旨 | Calcium homeostasis modulator (CALHM) family proteins are Ca-regulated adenosine triphosphate (ATP)-release channels involved in neural functions including neurotransmission in gustation. Here, we ...Calcium homeostasis modulator (CALHM) family proteins are Ca-regulated adenosine triphosphate (ATP)-release channels involved in neural functions including neurotransmission in gustation. Here, we present the cryo-electron microscopy (EM) structures of killifish CALHM1, human CALHM2, and CLHM-1 at resolutions of 2.66, 3.4, and 3.6 Å, respectively. The CALHM1 octamer structure reveals that the N-terminal helix forms the constriction site at the channel pore in the open state and modulates the ATP conductance. The CALHM2 undecamer and CLHM-1 nonamer structures show the different oligomeric stoichiometries among CALHM homologs. We further report the cryo-EM structures of the chimeric construct, revealing that the intersubunit interactions at the transmembrane domain (TMD) and the TMD-intracellular domain linker define the oligomeric stoichiometry. These findings advance our understanding of the ATP conduction and oligomerization mechanisms of CALHM channels. |
リンク | Sci Adv / PubMed:32832629 / PubMed Central |
手法 | EM (単粒子) |
解像度 | 2.66 - 3.6 Å |
構造データ | |
化合物 | ChemComp-Y01: |
由来 |
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キーワード | MEMBRANE PROTEIN / channel |