6VXM

Cryo-EM structure of Arabidopsis thaliana MSL1

6VXM の概要

• エントリーDOI: 10.2210/pdb6vxm/pdb
• EMDBエントリー: 21444 21445 21447
• 分子名称: Mechanosensitive ion channel protein 1, mitochondrial, EICOSANE (2 entities in total)
• 機能のキーワード: ion channel, transport protein
• 由来する生物種: Arabidopsis thaliana (Mouse-ear cress)
• タンパク質・核酸の鎖数: 7
• 化学式量合計: 331969.23

構造登録者

Deng, Z.,Zhang, J.,Yuan, P. (登録日: 2020-02-22, 公開日: 2020-08-05, 最終更新日: 2024-03-06)

主引用文献

Deng, Z.,Maksaev, G.,Schlegel, A.M.,Zhang, J.,Rau, M.,Fitzpatrick, J.A.J.,Haswell, E.S.,Yuan, P.
Structural mechanism for gating of a eukaryotic mechanosensitive channel of small conductance.
Nat Commun, 11:3690-3690, 2020

PubMed Abstract: Mechanosensitive ion channels transduce physical force into electrochemical signaling that underlies an array of fundamental physiological processes, including hearing, touch, proprioception, osmoregulation, and morphogenesis. The mechanosensitive channels of small conductance (MscS) constitute a remarkably diverse superfamily of channels critical for management of osmotic pressure. Here, we present cryo-electron microscopy structures of a MscS homolog from Arabidopsis thaliana, MSL1, presumably in both the closed and open states. The heptameric MSL1 channel contains an unusual bowl-shaped transmembrane region, which is reminiscent of the evolutionarily and architecturally unrelated mechanosensitive Piezo channels. Upon channel opening, the curved transmembrane domain of MSL1 flattens and expands. Our structures, in combination with functional analyses, delineate a structural mechanism by which mechanosensitive channels open under increased membrane tension. Further, the shared structural feature between unrelated channels suggests the possibility of a unified mechanical gating mechanism stemming from membrane deformation induced by a non-planar transmembrane domain.

PubMed: 32704140
DOI: 10.1038/s41467-020-17538-1

実験手法

ELECTRON MICROSCOPY (3.06 Å)