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- EMDB-9682: Structure of a plant cation channel -

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Basic information

Entry
Database: EMDB / ID: EMD-9682
TitleStructure of a plant cation channel
Map datacryo-EM map of a plant cation channel at 3.68 angstroms resolution
Sample
  • Cell: Plant chennel
    • Protein or peptide: Calcium permeable stress-gated cation channel 1
KeywordsChannel / MEMBRANE 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
CSC1/OSCA1-like, 7TM region / CSC1/OSCA1-like, cytosolic domain / CSC1/OSCA1-like, N-terminal transmembrane domain / Calcium permeable stress-gated cation channel 1-like / 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: 3.68 Å
AuthorsSun L / Wang J / Liu X
CitationJournal: Nat Commun / Year: 2018
Title: Structure of the hyperosmolality-gated calcium-permeable channel OSCA1.2.
Authors: Xin Liu / Jiawei Wang / Linfeng Sun /
Abstract: In plants, hyperosmolality stimuli triggers opening of the osmosensitive channels, leading to a rapid downstream signaling cascade initiated by cytosolic calcium concentration elevation. Members of ...In plants, hyperosmolality stimuli triggers opening of the osmosensitive channels, leading to a rapid downstream signaling cascade initiated by cytosolic calcium concentration elevation. Members of the OSCA family in Arabidopsis thaliana, identified as the hyperosmolality-gated calcium-permeable channels, have been suggested to play a key role during the initial phase of hyperosmotic stress response. Here, we report the atomic structure of Arabidopsis OSCA1.2 determined by single-particle cryo-electron microscopy. It contains 11 transmembrane helices and forms a homodimer. It is in an inactivated state, and the pore-lining residues are clearly identified. Its cytosolic domain contains a RNA recognition motif and two unique long helices. The linker between these two helices forms an anchor in the lipid bilayer and may be essential to osmosensing. The structure of AtOSCA1.2 serves as a platform for the study of the mechanism underlying osmotic stress responses and mechanosensing.
History
DepositionOct 12, 2018-
Header (metadata) releaseDec 12, 2018-
Map releaseDec 12, 2018-
UpdateMar 27, 2024-
Current statusMar 27, 2024Processing site: PDBj / Status: Released

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Structure visualization

Movie
  • Surface view with section colored by density value
  • Surface level: 0.1
  • Imaged by UCSF Chimera
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  • Surface view colored by cylindrical radius
  • Surface level: 0.1
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  • Surface view with fitted model
  • Atomic models: PDB-6ijz
  • Surface level: 0.1
  • Imaged by UCSF Chimera
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Movie viewer
Structure viewerEM map:
SurfViewMolmilJmol/JSmol
Supplemental images

emd_9682.png

Downloads & links

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Map

FileDownload / File: emd_9682.map.gz / Format: CCP4 / Size: 30.5 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Annotationcryo-EM map of a plant cation channel at 3.68 angstroms resolution
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
1.31 Å/pix.
x 200 pix.
= 261.4 Å		1.31 Å/pix.
x 200 pix.
= 261.4 Å		1.31 Å/pix.
x 200 pix.
= 261.4 Å

Surface

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 1.307 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 0.1 / Movie #1: 0.1
Minimum - Maximum-0.2663887 - 0.42128572
Average (Standard dev.)0.0006748489 (±0.013869367)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions200200200
Spacing200200200
CellA=B=C: 261.4 Å
α=β=γ: 90.0 °

CCP4 map header:

modeImage stored as Reals
Å/pix. X/Y/Z1.3071.3071.307
M x/y/z200200200
origin x/y/z0.0000.0000.000
length x/y/z261.400261.400261.400
α/β/γ90.00090.00090.000
start NX/NY/NZ000
NX/NY/NZ300300300
MAP C/R/S123
start NC/NR/NS000
NC/NR/NS200200200
D min/max/mean-0.2660.4210.001

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Supplemental data

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Sample components

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Entire : Plant chennel

EntireName: Plant chennel
Components
  • Cell: Plant chennel
    • Protein or peptide: Calcium permeable stress-gated cation channel 1

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Supramolecule #1: Plant chennel

SupramoleculeName: Plant chennel / type: cell / ID: 1 / Parent: 0 / Macromolecule list: all
Details: Protein expressed in Sf-9 cell and purified in digitonin
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: 87.985547 KDa
Recombinant expressionOrganism: Spodoptera frugiperda (fall armyworm)
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

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

Concentration5 mg/mL
BufferpH: 7.4
VitrificationCryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 281 K / Instrument: FEI VITROBOT MARK IV / Details: blot for 4 seconds before plunging.
DetailsThis sample was monodisperse.

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Electron microscopy

MicroscopeFEI TITAN KRIOS
Image recordingFilm or detector model: GATAN K2 SUMMIT (4k x 4k) / Detector mode: SUPER-RESOLUTION / Average exposure time: 8.0 sec. / Average electron dose: 50.0 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: SPOT SCAN / Imaging mode: BRIGHT FIELD
Sample stageSpecimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER / Cooling holder cryogen: NITROGEN
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

Startup modelType of model: OTHER
Final reconstructionApplied symmetry - Point group: C2 (2 fold cyclic) / Resolution.type: BY AUTHOR / Resolution: 3.68 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: RELION (ver. 2.0) / Number images used: 271802
Initial angle assignmentType: ANGULAR RECONSTITUTION / Software - Name: RELION (ver. 2.0)
Final angle assignmentType: MAXIMUM LIKELIHOOD / Software - Name: RELION (ver. 2.0)
Final 3D classificationSoftware - Name: RELION (ver. 2.0)

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Atomic model buiding 1

RefinementSpace: REAL / Protocol: AB INITIO MODEL
Output model

PDB-6ijz:
Structure of a plant cation channel

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