+Open data
-Basic information
Entry | Database: EMDB / ID: EMD-6822 | ||||||||||||
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Title | Structure of atOSCA1.1 channel | ||||||||||||
Map data | sharpened, used for model building | ||||||||||||
Sample |
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Function / homology | Function and homology information regulation of calcium ion import / calcium-activated cation channel activity / cellular hyperosmotic response / response to osmotic stress / monoatomic cation channel activity / protein tetramerization / plasma membrane / cytosol Similarity search - Function | ||||||||||||
Biological species | Arabidopsis thaliana (thale cress) | ||||||||||||
Method | single particle reconstruction / cryo EM / Resolution: 3.52 Å | ||||||||||||
Authors | Chen L / Zhang M / Kang Y / Wu JX | ||||||||||||
Funding support | China, 3 items
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Citation | Journal: Nat Struct Mol Biol / Year: 2018 Title: Structure of the mechanosensitive OSCA channels. Authors: Mingfeng Zhang / Dali Wang / Yunlu Kang / Jing-Xiang Wu / Fuqiang Yao / Chengfang Pan / Zhiqiang Yan / Chen Song / Lei Chen / Abstract: Mechanosensitive ion channels convert mechanical stimuli into a flow of ions. These channels are widely distributed from bacteria to higher plants and humans, and are involved in many crucial ...Mechanosensitive ion channels convert mechanical stimuli into a flow of ions. These channels are widely distributed from bacteria to higher plants and humans, and are involved in many crucial physiological processes. Here we show that two members of the OSCA protein family in Arabidopsis thaliana, namely AtOSCA1.1 and AtOSCA3.1, belong to a new class of mechanosensitive ion channels. We solve the structure of the AtOSCA1.1 channel at 3.5-Å resolution and AtOSCA3.1 at 4.8-Å resolution by cryo-electron microscopy. OSCA channels are symmetric dimers that are mediated by cytosolic inter-subunit interactions. Strikingly, they have structural similarity to the mammalian TMEM16 family proteins. Our structural analysis accompanied with electrophysiological studies identifies the ion permeation pathway within each subunit and suggests a conformational change model for activation. | ||||||||||||
History |
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-Structure visualization
Movie |
Movie viewer |
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Structure viewer | EM map: SurfViewMolmilJmol/JSmol |
Supplemental images |
-Downloads & links
-EMDB archive
Map data | emd_6822.map.gz | 59.4 MB | EMDB map data format | |
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Header (meta data) | emd-6822-v30.xml emd-6822.xml | 16.3 KB 16.3 KB | Display Display | EMDB header |
Images | emd_6822.png | 223.3 KB | ||
Masks | emd_6822_msk_1.map | 64 MB | Mask map | |
Others | emd_6822_half_map_1.map.gz emd_6822_half_map_2.map.gz | 59.2 MB 59.2 MB | ||
Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-6822 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-6822 | HTTPS FTP |
-Validation report
Summary document | emd_6822_validation.pdf.gz | 879 KB | Display | EMDB validaton report |
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Full document | emd_6822_full_validation.pdf.gz | 878.6 KB | Display | |
Data in XML | emd_6822_validation.xml.gz | 11.3 KB | Display | |
Data in CIF | emd_6822_validation.cif.gz | 13.3 KB | Display | |
Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-6822 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-6822 | HTTPS FTP |
-Related structure data
Related structure data | 6jpfMC 6875C 5z1fC M: atomic model generated by this map C: citing same article (ref.) |
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Similar structure data |
-Links
EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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-Map
File | Download / File: emd_6822.map.gz / Format: CCP4 / Size: 64 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Annotation | sharpened, used for model building | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 1 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
CCP4 map header:
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-Supplemental data
-Mask #1
File | emd_6822_msk_1.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Half map: #1
File | emd_6822_half_map_1.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Half map: #2
File | emd_6822_half_map_2.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Sample components
-Entire : atOSCA1.1
Entire | Name: atOSCA1.1 |
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Components |
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-Supramolecule #1: atOSCA1.1
Supramolecule | Name: atOSCA1.1 / type: complex / ID: 1 / Parent: 0 / Macromolecule list: all |
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Source (natural) | Organism: Arabidopsis thaliana (thale cress) |
Recombinant expression | Organism: Homo sapiens (human) |
Molecular weight | Theoretical: 175 KDa |
-Macromolecule #1: Protein OSCA1
Macromolecule | Name: Protein OSCA1 / type: protein_or_peptide / ID: 1 / Number of copies: 2 / Enantiomer: LEVO |
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Source (natural) | Organism: Arabidopsis thaliana (thale cress) |
Molecular weight | Theoretical: 87.697008 KDa |
Recombinant expression | Organism: Homo sapiens (human) |
Sequence | String: MATLKDIGVS AGINILTAFI FFIIFAFLRL QPFNDRVYFS KWYLRGLRSS PASGGGFAGR FVNLELRSYL KFLHWMPEAL KMPERELID HAGLDSVVYL RIYWLGLKIF APIAMLAWAV LVPVNWTNNE LELAKHFKNV TSSDIDKLTI SNIPEGSNRF W AHIIMAYA ...String: MATLKDIGVS AGINILTAFI FFIIFAFLRL QPFNDRVYFS KWYLRGLRSS PASGGGFAGR FVNLELRSYL KFLHWMPEAL KMPERELID HAGLDSVVYL RIYWLGLKIF APIAMLAWAV LVPVNWTNNE LELAKHFKNV TSSDIDKLTI SNIPEGSNRF W AHIIMAYA FTIWTCYMLM KEYETVANMR LQFLASEGRR PDQFTVLVRN VPPDPDETVS ELVEHFFLVN HPDNYLTHQV VC NANKLAD LVSKKTKLQN WLDYYQLKYT RNNSQIRPIT KLGCLGLCGQ KVDAIEHYIA EVDKTSKEIA EERENVVNDQ KSV MPASFV SFKTRWAAAV CAQTTQTRNP TEWLTEWAAE PRDIYWPNLA IPYVSLTVRR LVMNVAFFFL TFFFIIPIAF VQSL ATIEG IEKVAPFLKV IIEKDFIKSL IQGLLAGIAL KLFLIFLPAI LMTMSKFEGF TSVSFLERRS ASRYYIFNLV NVFLG SVIA GAAFEQLNSF LNQSPNQIPK TIGMAIPMKA TFFITYIMVD GWAGVAGEIL MLKPLIIYHL KNAFLVKTEK DREEAM NPG SIGFNTGEPQ IQLYFLLGLV YAPVTPMLLP FILVFFALAY VVYRHQIINV YNQEYESAAA FWPDVHGRVI TALIISQ LL LMGLLGTKHA ASAAPFLIAL PVITIGFHRF CKGRFEPAFV RYPLQEAMMK DTLERAREPN LNLKGYLQDA YIHPVFKG G DNDDDGDMIG KLENEVIIVP TKRQSRRNTP APSRISGESS PSLAVINGKE V |
-Experimental details
-Structure determination
Method | cryo EM |
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Processing | single particle reconstruction |
Aggregation state | particle |
-Sample preparation
Buffer | pH: 8 |
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Vitrification | Cryogen name: ETHANE |
-Electron microscopy
Microscope | FEI TITAN KRIOS |
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Image recording | Film or detector model: GATAN K2 SUMMIT (4k x 4k) / Average electron dose: 50.0 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
Electron optics | C2 aperture diameter: 100.0 µm / Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Cs: 0.01 mm |
Experimental equipment | Model: Titan Krios / Image courtesy: FEI Company |
+Image processing
-Atomic model buiding 1
Refinement | Space: REAL / Protocol: AB INITIO MODEL |
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Output model | PDB-6jpf: |