- EMDB-41166: Cryo-EM structure of the wild-type AtMSL10 in saposin -
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基本情報
登録情報
データベース: EMDB / ID: EMD-41166
タイトル
Cryo-EM structure of the wild-type AtMSL10 in saposin
マップデータ
NU-refinement
試料
複合体: AtMSL10 in saposin
タンパク質・ペプチド: Mechanosensitive ion channel protein 10
キーワード
ion channels / mechanosensitive channels / heptamer / Arabidopsis thaliana / TRANSPORT PROTEIN
機能・相同性
機能・相同性情報
programmed cell death in response to reactive oxygen species / leaf senescence / detection of mechanical stimulus / mechanosensitive monoatomic ion channel activity / monoatomic anion transport / plasma membrane 類似検索 - 分子機能
Mechanosensitive ion channel MscS-like, plants/fungi / Mechanosensitive ion channel MscS / Mechanosensitive ion channel, beta-domain / Mechanosensitive ion channel MscS, beta-domain superfamily / LSM domain superfamily 類似検索 - ドメイン・相同性
Mechanosensitive ion channel protein 10 類似検索 - 構成要素
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)
R01 GM143440
米国
引用
ジャーナル: Nat Commun / 年: 2023 タイトル: Open structure and gating of the Arabidopsis mechanosensitive ion channel MSL10. 著者: Jingying Zhang / Grigory Maksaev / Peng Yuan / 要旨: Plants are challenged by drastically different osmotic environments during growth and development. Adaptation to these environments often involves mechanosensitive ion channels that can detect and ...Plants are challenged by drastically different osmotic environments during growth and development. Adaptation to these environments often involves mechanosensitive ion channels that can detect and respond to mechanical force. In the model plant Arabidopsis thaliana, the mechanosensitive channel MSL10 plays a crucial role in hypo-osmotic shock adaptation and programmed cell death induction, but the molecular basis of channel function remains poorly understood. Here, we report a structural and electrophysiological analysis of MSL10. The cryo-electron microscopy structures reveal a distinct heptameric channel assembly. Structures of the wild-type channel in detergent and lipid environments, and in the absence of membrane tension, capture an open conformation. Furthermore, structural analysis of a non-conductive mutant channel demonstrates that reorientation of phenylalanine side chains alone, without main chain rearrangements, may generate the hydrophobic gate. Together, these results reveal a distinct gating mechanism and advance our understanding of mechanotransduction.