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- EMDB-38503: Cryo-EM structure of OSCA1.2-liposome-inside-out closed state -

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Basic information

Entry
Database: EMDB / ID: EMD-38503
TitleCryo-EM structure of OSCA1.2-liposome-inside-out closed state
Map data
Sample
  • Complex: Cryo-EM structure of OSCA1.2-liposome-inside-out closed state
    • Protein or peptide: Calcium permeable stress-gated cation channel 1
KeywordsOSCA/TMEM63 channel / mechanosensitive channel / PLANT PROTEIN
Function / homology
Function and homology information


mechanosensitive monoatomic ion channel activity / calcium-activated cation channel activity / monoatomic cation transport / identical protein binding / plasma membrane
Similarity search - Function
Calcium permeable stress-gated cation channel 1-like / CSC1/OSCA1-like, 7TM region / CSC1/OSCA1-like, cytosolic domain / CSC1/OSCA1-like, N-terminal transmembrane domain / Calcium-dependent channel, 7TM region, putative phosphate / Late exocytosis, associated with Golgi transport / Cytosolic domain of 10TM putative phosphate transporter
Similarity search - Domain/homology
Calcium permeable stress-gated cation channel 1
Similarity search - Component
Biological speciesArabidopsis thaliana (thale cress)
Methodsingle particle reconstruction / cryo EM / Resolution: 3.56 Å
AuthorsZhang Y / Han Y
Funding support China, Australia, 3 items
OrganizationGrant numberCountry
Ministry of Science and Technology (MoST, China)2022ZD0207400 China
Australian Research Council (ARC)FT220100159 Australia
Australian Research Council (ARC)DP200100860 Australia
CitationJournal: Nature / Year: 2024
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
DepositionDec 29, 2023-
Header (metadata) releaseApr 10, 2024-
Map releaseApr 10, 2024-
UpdateApr 17, 2024-
Current statusApr 17, 2024Processing site: PDBj / Status: Released

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Structure visualization

Supplemental images

emd_38503.png

Downloads & links

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Map

FileDownload / File: emd_38503.map.gz / Format: CCP4 / Size: 52.7 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Voxel sizeX=Y=Z: 1.055 Å
Density
Contour LevelBy AUTHOR: 0.305
Minimum - Maximum-0.9600706 - 1.498336
Average (Standard dev.)0.012204901 (±0.062807485)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions240240240
Spacing240240240
CellA=B=C: 253.19998 Å
α=β=γ: 90.0 °

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Supplemental data

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Half map: #2

Fileemd_38503_half_map_1.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Half map: #1

Fileemd_38503_half_map_2.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Sample components

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Entire : Cryo-EM structure of OSCA1.2-liposome-inside-out closed state

EntireName: Cryo-EM structure of OSCA1.2-liposome-inside-out closed state
Components
  • Complex: Cryo-EM structure of OSCA1.2-liposome-inside-out closed state
    • Protein or peptide: Calcium permeable stress-gated cation channel 1

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Supramolecule #1: Cryo-EM structure of OSCA1.2-liposome-inside-out closed state

SupramoleculeName: Cryo-EM structure of OSCA1.2-liposome-inside-out closed state
type: complex / ID: 1 / Parent: 0 / Macromolecule list: all
Source (natural)Organism: Arabidopsis thaliana (thale cress)

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Macromolecule #1: Calcium permeable stress-gated cation channel 1

MacromoleculeName: Calcium permeable stress-gated cation channel 1 / type: protein_or_peptide / ID: 1 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Arabidopsis thaliana (thale cress)
Molecular weightTheoretical: 89.003664 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString: 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 SNSLEVLFQ

UniProtKB: Calcium permeable stress-gated cation channel 1

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Experimental details

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Structure determination

Methodcryo EM
Processingsingle particle reconstruction
Aggregation stateparticle

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Sample preparation

BufferpH: 7.9
VitrificationCryogen name: ETHANE

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Electron microscopy

MicroscopeFEI TITAN KRIOS
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELDBright-field microscopy / Nominal defocus max: 2.4 µm / Nominal defocus min: 1.4000000000000001 µm
Image recordingFilm or detector model: GATAN K3 (6k x 4k) / Average electron dose: 49.41 e/Å2
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

Startup modelType of model: PDB ENTRY
PDB model - PDB ID:

6mgv

Initial angle assignmentType: MAXIMUM LIKELIHOOD
Final angle assignmentType: MAXIMUM LIKELIHOOD
Final reconstructionResolution.type: BY AUTHOR / Resolution: 3.56 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 100731

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