5Z10
Structure of the mechanosensitive Piezo1 channel
5Z10 の概要
| エントリーDOI | 10.2210/pdb5z10/pdb |
| EMDBエントリー | 6865 |
| 分子名称 | Piezo-type mechanosensitive ion channel component 1 (1 entity in total) |
| 機能のキーワード | piezo1, piezo2, mechanogating, channel, membrane protein |
| 由来する生物種 | Mus musculus (Mouse) |
| タンパク質・核酸の鎖数 | 3 |
| 化学式量合計 | 876961.97 |
| 構造登録者 | |
| 主引用文献 | Zhao, Q.,Zhou, H.,Chi, S.,Wang, Y.,Wang, J.,Geng, J.,Wu, K.,Liu, W.,Zhang, T.,Dong, M.Q.,Wang, J.,Li, X.,Xiao, B. Structure and mechanogating mechanism of the Piezo1 channel. Nature, 554:487-492, 2018 Cited by PubMed Abstract: The mechanosensitive Piezo channels function as key eukaryotic mechanotransducers. However, their structures and mechanogating mechanisms remain unknown. Here we determine the three-bladed, propeller-like electron cryo-microscopy structure of mouse Piezo1 and functionally reveal its mechanotransduction components. Despite the lack of sequence repetition, we identify nine repetitive units consisting of four transmembrane helices each-which we term transmembrane helical units (THUs)-which assemble into a highly curved blade-like structure. The last transmembrane helix encloses a hydrophobic pore, followed by three intracellular fenestration sites and side portals that contain pore-property-determining residues. The central region forms a 90 Å-long intracellular beam-like structure, which undergoes a lever-like motion to connect THUs to the pore via the interfaces of the C-terminal domain, the anchor-resembling domain and the outer helix. Deleting extracellular loops in the distal THUs or mutating single residues in the beam impairs the mechanical activation of Piezo1. Overall, Piezo1 possesses a unique 38-transmembrane-helix topology and designated mechanotransduction components, which enable a lever-like mechanogating mechanism. PubMed: 29469092DOI: 10.1038/nature25743 主引用文献が同じPDBエントリー |
| 実験手法 | ELECTRON MICROSCOPY (3.97 Å) |
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