7USX

Structure of Contracted C. elegans TMC-1 complex

7USX の概要

• エントリーDOI: 10.2210/pdb7usx/pdb
• EMDBエントリー: 26741 26742 26743
• 分子名称: Transmembrane channel-like protein 1, 1,2-Distearoyl-sn-glycerophosphoethanolamine, PALMITIC ACID, ... (11 entities in total)
• 機能のキーワード: complex, membrane protein
• 由来する生物種: Caenorhabditis elegans; 詳細
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 379265.54

構造登録者

Jeong, H.,Clark, S.,Gouaux, E. (登録日: 2022-04-26, 公開日: 2022-10-19, 最終更新日: 2023-08-09)

主引用文献

Jeong, H.,Clark, S.,Goehring, A.,Dehghani-Ghahnaviyeh, S.,Rasouli, A.,Tajkhorshid, E.,Gouaux, E.
Structures of the TMC-1 complex illuminate mechanosensory transduction.
Nature, 610:796-803, 2022

PubMed Abstract: The initial step in the sensory transduction pathway underpinning hearing and balance in mammals involves the conversion of force into the gating of a mechanosensory transduction channel. Despite the profound socioeconomic impacts of hearing disorders and the fundamental biological significance of understanding mechanosensory transduction, the composition, structure and mechanism of the mechanosensory transduction complex have remained poorly characterized. Here we report the single-particle cryo-electron microscopy structure of the native transmembrane channel-like protein 1 (TMC-1) mechanosensory transduction complex isolated from Caenorhabditis elegans. The two-fold symmetric complex is composed of two copies each of the pore-forming TMC-1 subunit, the calcium-binding protein CALM-1 and the transmembrane inner ear protein TMIE. CALM-1 makes extensive contacts with the cytoplasmic face of the TMC-1 subunits, whereas the single-pass TMIE subunits reside on the periphery of the complex, poised like the handles of an accordion. A subset of complexes additionally includes a single arrestin-like protein, arrestin domain protein (ARRD-6), bound to a CALM-1 subunit. Single-particle reconstructions and molecular dynamics simulations show how the mechanosensory transduction complex deforms the membrane bilayer and suggest crucial roles for lipid-protein interactions in the mechanism by which mechanical force is transduced to ion channel gating.

PubMed: 36224384
DOI: 10.1038/s41586-022-05314-8

実験手法

ELECTRON MICROSCOPY (3.09 Å)