6MGV

Structure of mechanically activated ion channel OSCA1.2 in nanodisc

Summary for 6MGV

• Entry DOI: 10.2210/pdb6mgv/pdb
• Related: 6MGW
• EMDB information: 9112 9113
• Descriptor: Calcium permeable stress-gated cation channel 1 (1 entity in total)
• Functional Keywords: mechanically activated ion channel, membrane protein
• Biological source: Arabidopsis thaliana (Mouse-ear cress)
• Total number of polymer chains: 2
• Total formula weight: 178063.44

Authors

Jojoa-Cruz, S.,Saotome, K.,Patapoutian, A.,Ward, A.B. (deposition date: 2018-09-15, release date: 2018-11-14, Last modification date: 2024-03-13)

Primary citation

Jojoa Cruz, S.,Saotome, K.,Murthy, S.E.,Tsui, C.C.A.,Sansom, M.S.,Patapoutian, A.,Ward, A.B.
Cryo-EM structure of the mechanically activated ion channel OSCA1.2.
Elife, 7:-, 2018

PubMed Abstract: Mechanically activated ion channels underlie touch, hearing, shear-stress sensing, and response to turgor pressure. OSCA/TMEM63s are a newly-identified family of eukaryotic mechanically activated ion channels opened by membrane tension. The structural underpinnings of OSCA/TMEM63 function are not explored. Here, we elucidate high resolution cryo-electron microscopy structures of OSCA1.2, revealing a dimeric architecture containing eleven transmembrane helices per subunit and surprising topological similarities to TMEM16 proteins. We locate the ion permeation pathway within each subunit by demonstrating that a conserved acidic residue is a determinant of channel conductance. Molecular dynamics simulations reveal membrane interactions, suggesting the role of lipids in OSCA1.2 gating. These results lay a foundation to decipher how the structural organization of OSCA/TMEM63 is suited for their roles as MA ion channels.

PubMed: 30382939
DOI: 10.7554/eLife.41845

Experimental method

ELECTRON MICROSCOPY (3.1 Å)