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Open data
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Basic information
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Title | Cryo-EM structure of TMEM63B-Digitonin state | ||||||||||||
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![]() | OSCA/TMEM63 channel / mechanosensitive channel / PLANT PROTEIN | ||||||||||||
Function / homology | ![]() alveolar lamellar body membrane / surfactant secretion / osmolarity-sensing monoatomic cation channel activity / mechanosensitive monoatomic cation channel activity / mechanosensitive monoatomic ion channel activity / calcium-activated cation channel activity / sensory perception of sound / actin cytoskeleton / early endosome membrane / plasma membrane Similarity search - Function | ||||||||||||
Biological species | ![]() | ||||||||||||
Method | single particle reconstruction / cryo EM / Resolution: 3.84 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 | ![]() | 61.4 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 14.8 KB 14.8 KB | Display Display | ![]() |
Images | ![]() | 97.9 KB | ||
Filedesc metadata | ![]() | 5.7 KB | ||
Others | ![]() ![]() | 60.6 MB 60.6 MB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 8xw4MC ![]() 8xajC ![]() 8xngC ![]() 8xryC ![]() 8xs0C ![]() 8xs4C ![]() 8xs5C ![]() 8xvxC ![]() 8xvyC ![]() 8xvzC ![]() 8xw0C ![]() 8xw1C ![]() 8xw2C ![]() 8xw3C C: citing same article ( M: atomic model generated by this map |
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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: 0.83 Å | ||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
-Half map: #2
File | emd_38730_half_map_1.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Half map: #1
File | emd_38730_half_map_2.map | ||||||||||||
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Density Histograms |
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Sample components
-Entire : Cryo-EM structure of TMEM63B-Digitonin state
Entire | Name: Cryo-EM structure of TMEM63B-Digitonin state |
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Components |
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-Supramolecule #1: Cryo-EM structure of TMEM63B-Digitonin state
Supramolecule | Name: Cryo-EM structure of TMEM63B-Digitonin state / type: complex / ID: 1 / Parent: 0 / Macromolecule list: all |
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Source (natural) | Organism: ![]() |
-Macromolecule #1: CSC1-like protein 2
Macromolecule | Name: CSC1-like protein 2 / type: protein_or_peptide / ID: 1 / Number of copies: 1 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 96.506609 KDa |
Recombinant expression | Organism: ![]() |
Sequence | String: MLPFLLATLG TTALNNSNPK DYCYSARIRS TVLQGLPFGG VPTVLALDFM CFLALLFLFS ILRKVAWDYG RLALVTDADR LRRQERDRV EQEYVASAMH GDSHDRYERL TSVSSSVDFD QRDNGFCSWL TAIFRIKDDE IRDKCGGDAV HYLSFQRHII G LLVVVGVL ...String: MLPFLLATLG TTALNNSNPK DYCYSARIRS TVLQGLPFGG VPTVLALDFM CFLALLFLFS ILRKVAWDYG RLALVTDADR LRRQERDRV EQEYVASAMH GDSHDRYERL TSVSSSVDFD QRDNGFCSWL TAIFRIKDDE IRDKCGGDAV HYLSFQRHII G LLVVVGVL SVGIVLPVNF SGDLLENNAY SFGRTTIANL KSGNNLLWLH TSFAFLYLLL TVYSMRRHTS KMRYKEDDLV KR TLFINGI SKYAESEKIK KHFEEAYPNC TVLEARPCYN VARLMFLDAE RKKAERGKLY FTNLQSKENV PTMINPKPCG HLC CCVVRG CEQVEAIEYY TKLEQKLKED YKREKEKVNE KPLGMAFVTF HNETITAIIL KDFNVCKCQG CTCRGEPRPS SCSE SLHIS NWTVSYAPDP QNIYWEHLSI RGFIWWLRCL VINVVLFILL FFLTTPAIII TTMDKFNVTK PVEYLNNPII TQFFP TLLL WCFSALLPTI VYYSAFFEAH WTRSGENRTT MHKCYTFLIF MVLLLPSLGL SSLDLFFRWL FDKKFLAEAA IRFECV FLP DNGAFFVNYV IASAFIGNAM DLLRIPGLLM YMIRLCLARS AAERRNVKRH QAYEFQFGAA YAWMMCVFTV VMTYSIT CP IIVPFGLMYM LLKHLVDRYN LYYAYLPAKL DKKIHSGAVN QVVAAPILCL FWLLFFSTMR TGFLAPTSMF TFVVLVIT I VICLCHVCFG HFKYLSAHNY KIEHTETDTV DPRSNGRPPT AAAVPKSAKY IAQVLQDSEV DGDGDGAPGS SGDEPPSSS SQDEELLMPP DALTDTDFQS CEDSLIENEI HQSNSWSHPQ FEKL UniProtKB: CSC1-like protein 2 |
-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: 63.8 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: OTHER |
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Final reconstruction | Resolution.type: BY AUTHOR / Resolution: 3.84 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 378646 |
Initial angle assignment | Type: MAXIMUM LIKELIHOOD |
Final angle assignment | Type: MAXIMUM LIKELIHOOD |