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6VXN

Cryo-EM structure of Arabidopsis thaliana MSL1 A320V

Summary for 6VXN
Entry DOI10.2210/pdb6vxn/pdb
EMDB information21444 21445 21447
DescriptorMechanosensitive ion channel protein 1, mitochondrial, DODECANE (2 entities in total)
Functional Keywordsion channel, transport protein
Biological sourceArabidopsis thaliana (Mouse-ear cress)
Total number of polymer chains7
Total formula weight327424.45
Authors
Deng, Z.,Zhang, J.,Yuan, P. (deposition date: 2020-02-22, release date: 2020-08-05, Last modification date: 2024-03-06)
Primary citationDeng, 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
Cited by
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
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (2.96 Å)
Structure validation

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