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Open data
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Basic information
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Title | Cryo-EM structure of OSCA1.2-liposome-inside-in open state | ||||||||||||
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![]() | OSCA/TMEM63 channel / mechanosensitive channel / PLANT PROTEIN | ||||||||||||
Function / homology | ![]() mechanosensitive monoatomic ion channel activity / calcium-activated cation channel activity / monoatomic cation transport / identical protein binding / plasma membrane Similarity search - Function | ||||||||||||
Biological species | ![]() ![]() | ||||||||||||
Method | single particle reconstruction / cryo EM / Resolution: 3.29 Å | ||||||||||||
![]() | Zhang Y / Han Y | ||||||||||||
Funding support | ![]() ![]()
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![]() | ![]() Title: Mechanical activation opens a lipid-lined pore in OSCA ion channels. Authors: Yaoyao Han / Zijing Zhou / Ruitao Jin / Fei Dai / Yifan Ge / Xisan Ju / Xiaonuo Ma / Sitong He / Ling Yuan / Yingying Wang / Wei Yang / Xiaomin Yue / Zhongwen Chen / Yadong Sun / Ben Corry / ...Authors: Yaoyao Han / Zijing Zhou / Ruitao Jin / Fei Dai / Yifan Ge / Xisan Ju / Xiaonuo Ma / Sitong He / Ling Yuan / Yingying Wang / Wei Yang / Xiaomin Yue / Zhongwen Chen / Yadong Sun / Ben Corry / Charles D Cox / Yixiao Zhang / ![]() ![]() Abstract: OSCA/TMEM63 channels are the largest known family of mechanosensitive channels, playing critical roles in plant and mammalian mechanotransduction. Here we determined 44 cryogenic electron microscopy ...OSCA/TMEM63 channels are the largest known family of mechanosensitive channels, playing critical roles in plant and mammalian mechanotransduction. Here we determined 44 cryogenic electron microscopy structures of OSCA/TMEM63 channels in different environments to investigate the molecular basis of OSCA/TMEM63 channel mechanosensitivity. In nanodiscs, we mimicked increased membrane tension and observed a dilated pore with membrane access in one of the OSCA1.2 subunits. In liposomes, we captured the fully open structure of OSCA1.2 in the inside-in orientation, in which the pore shows a large lateral opening to the membrane. Unusually for ion channels, structural, functional and computational evidence supports the existence of a 'proteo-lipidic pore' in which lipids act as a wall of the ion permeation pathway. In the less tension-sensitive homologue OSCA3.1, we identified an 'interlocking' lipid tightly bound in the central cleft, keeping the channel closed. Mutation of the lipid-coordinating residues induced OSCA3.1 activation, revealing a conserved open conformation of OSCA channels. Our structures provide a global picture of the OSCA channel gating cycle, uncover the importance of bound lipids and show that each subunit can open independently. This expands both our understanding of channel-mediated mechanotransduction and channel pore formation, with important mechanistic implications for the TMEM16 and TMC protein families. | ||||||||||||
History |
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Structure visualization
Supplemental images |
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Downloads & links
-EMDB archive
Map data | ![]() | 8.4 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 17.2 KB 17.2 KB | Display Display | ![]() |
Images | ![]() | 78.2 KB | ||
Filedesc metadata | ![]() | 6 KB | ||
Others | ![]() ![]() ![]() | 48.1 MB 42.5 MB 42.5 MB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 8xajMC ![]() 8xngC ![]() 8xryC ![]() 8xs0C ![]() 8xs4C ![]() 8xs5C ![]() 8xvxC ![]() 8xvyC ![]() 8xvzC ![]() 8xw0C ![]() 8xw1C ![]() 8xw2C ![]() 8xw3C ![]() 8xw4C M: atomic model generated by this map C: citing same article ( |
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Similar structure data | Similarity search - Function & homology ![]() |
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Links
EMDB pages | ![]() ![]() |
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Map
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Voxel size | X=Y=Z: 1.055 Å | ||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
-Additional map: #1
File | emd_38200_additional_1.map | ||||||||||||
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Density Histograms |
-Half map: #2
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Density Histograms |
-Half map: #1
File | emd_38200_half_map_2.map | ||||||||||||
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Density Histograms |
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Sample components
-Entire : The cryo-EM structure of OSCA1.2-liposome-inside-in open state
Entire | Name: The cryo-EM structure of OSCA1.2-liposome-inside-in open state |
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Components |
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-Supramolecule #1: The cryo-EM structure of OSCA1.2-liposome-inside-in open state
Supramolecule | Name: The cryo-EM structure of OSCA1.2-liposome-inside-in open state type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1 |
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Source (natural) | Organism: ![]() ![]() |
-Macromolecule #1: Calcium permeable stress-gated cation channel 1
Macromolecule | Name: Calcium permeable stress-gated cation channel 1 / type: protein_or_peptide / ID: 1 / Number of copies: 2 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() ![]() |
Molecular weight | Theoretical: 87.985547 KDa |
Recombinant expression | Organism: ![]() |
Sequence | String: MATLQDIGVS AGINILSAFV FFIIFAVLRL QPFNDRVYFS KWYLKGLRSS PARGGAFAQR FVNLDFRSYM KFLNWMPEAL KMPEPELID HAGLDSVVYL RIYWLGLKIF TPIAVLAWAV LVPVNWTNNT LEMAKQLRNV TSSDIDKLSV SNIPEYSMRF W THIVMAYA ...String: MATLQDIGVS AGINILSAFV FFIIFAVLRL QPFNDRVYFS KWYLKGLRSS PARGGAFAQR FVNLDFRSYM KFLNWMPEAL KMPEPELID HAGLDSVVYL RIYWLGLKIF TPIAVLAWAV LVPVNWTNNT LEMAKQLRNV TSSDIDKLSV SNIPEYSMRF W THIVMAYA FTIWTCYVLM KEYETIANMR LQFVASEARR PDQFTVLVRN VPPDADESVS ELVEHFFLVN HPDHYLTHQV VC NANKLAD LVKKKKKLQN WLDYYQLKYA RNNSQRIMVK LGFLGLWGQK VDAIEHYIAE IDKISKEISK EREEVVNDPK AIM PAAFVS FKTRWAAAVC AQTQQTRNPT QWLTEWAPEP RDVFWSNLAI PYVSLTVRRL IMHVAFFFLT FFFIVPIAFV QSLA TIEGI VKAAPFLKFI VDDKFMKSVI QGFLPGIALK LFLAFLPSIL MIMSKFEGFT SISSLERRAA FRYYIFNLVN VFLAS VIAG AAFEQLNSFL NQSANQIPKT IGVAIPMKAT FFITYIMVDG WAGVAGEILM LKPLIMFHLK NAFLVKTDKD REEAMD PGS IGFNTGEPRI QLYFLLGLVY APVTPMLLPF ILVFFALAYI VYRHQIINVY NQEYESAAAF WPDVHGRVIA ALVISQL LL MGLLGTKHAA LAAPFLIALP VLTIGFHHFC KGRYEPAFIR YPLQEAMMKD TLETAREPNL NLKGYLQNAY VHPVFKGD E DDYDIDDKLG KFEDEAIIVP TKRQSRRNTP APSIISGDDS PSLPFSGKLV UniProtKB: Calcium permeable stress-gated cation channel 1 |
-Macromolecule #2: 1,2-DIOLEOYL-SN-GLYCERO-3-PHOSPHOCHOLINE
Macromolecule | Name: 1,2-DIOLEOYL-SN-GLYCERO-3-PHOSPHOCHOLINE / type: ligand / ID: 2 / Number of copies: 7 / Formula: PCW |
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Molecular weight | Theoretical: 787.121 Da |
Chemical component information | ![]() ChemComp-PCW: |
-Experimental details
-Structure determination
Method | cryo EM |
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![]() | single particle reconstruction |
Aggregation state | particle |
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Sample preparation
Buffer | pH: 7.9 |
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Vitrification | Cryogen name: ETHANE |
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Electron microscopy
Microscope | FEI TITAN KRIOS |
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Image recording | Film or detector model: GATAN K3 (6k x 4k) / Average electron dose: 49.41 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: ![]() |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 2.4 µm / Nominal defocus min: 1.4000000000000001 µm |
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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Image processing
Startup model | Type of model: PDB ENTRY PDB model - PDB ID: |
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Final reconstruction | Resolution.type: BY AUTHOR / Resolution: 3.29 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 269163 |
Initial angle assignment | Type: MAXIMUM LIKELIHOOD |
Final angle assignment | Type: MAXIMUM LIKELIHOOD |