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Open data
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Basic information
Entry | Database: EMDB / ID: EMD-22343 | |||||||||
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Title | Cryo-EM structure of a proton-activated chloride channel | |||||||||
![]() | Cryo-EM structure of a proton-activated chloride channel | |||||||||
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Function / homology | TMEM206 protein / TMEM206 protein family / membrane => GO:0016020 / plasma membrane / Proton-activated chloride channel![]() | |||||||||
Biological species | ![]() ![]() ![]() ![]() | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 3.46 Å | |||||||||
![]() | Deng Z / Zhang J / Yuan P | |||||||||
![]() | ![]() Title: Cryo-EM structure of a proton-activated chloride channel TMEM206. Authors: Zengqin Deng / Yonghui Zhao / Jing Feng / Jingying Zhang / Haiyan Zhao / Michael J Rau / James A J Fitzpatrick / Hongzhen Hu / Peng Yuan / ![]() Abstract: TMEM206 has been recently identified as an evolutionarily conserved chloride channel that underlies ubiquitously expressed, proton-activated, outwardly rectifying anion currents. Here, we report the ...TMEM206 has been recently identified as an evolutionarily conserved chloride channel that underlies ubiquitously expressed, proton-activated, outwardly rectifying anion currents. Here, we report the cryo-electron microscopy structure of pufferfish TMEM206, which forms a trimeric channel, with each subunit comprising two transmembrane segments and a large extracellular domain. An ample vestibule in the extracellular region is accessible laterally from the three side portals. The central pore contains multiple constrictions. A conserved lysine residue near the cytoplasmic end of the inner helix forms the presumed chloride ion selectivity filter. Unprecedentedly, the core structure and assembly closely resemble those of the epithelial sodium channel/degenerin family of sodium channels that are unrelated in amino acid sequence and conduct cations instead of anions. Together with electrophysiology, this work provides insights into ion conduction and gating for a new class of chloride channels that is architecturally distinct from previously characterized chloride channel families. | |||||||||
History |
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Structure visualization
Movie |
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Structure viewer | EM map: ![]() ![]() ![]() |
Supplemental images |
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Downloads & links
-EMDB archive
Map data | ![]() | 30.9 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 9.4 KB 9.4 KB | Display Display | ![]() |
Images | ![]() | 49.6 KB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Validation report
Summary document | ![]() | 382.3 KB | Display | ![]() |
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Full document | ![]() | 381.8 KB | Display | |
Data in XML | ![]() | 5.7 KB | Display | |
Data in CIF | ![]() | 6.5 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 7ji3MC M: atomic model generated by this map C: citing same article ( |
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Similar structure data |
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Links
EMDB pages | ![]() ![]() |
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Map
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Annotation | Cryo-EM structure of a proton-activated chloride channel | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 1.1 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
CCP4 map header:
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-Supplemental data
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Sample components
-Entire : TMEM206
Entire | Name: TMEM206 |
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Components |
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-Supramolecule #1: TMEM206
Supramolecule | Name: TMEM206 / type: complex / ID: 1 / Parent: 0 / Macromolecule list: all |
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Source (natural) | Organism: ![]() ![]() |
Recombinant expression | Organism: ![]() |
-Macromolecule #1: Proton-activated chloride channel
Macromolecule | Name: Proton-activated chloride channel / type: protein_or_peptide / ID: 1 / Number of copies: 3 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() ![]() |
Molecular weight | Theoretical: 52.907641 KDa |
Recombinant expression | Organism: ![]() |
Sequence | String: MRRNSYREFI DEDDEDDGNK DVPNCFDDVI DSPEEVEPND SASPDDDNRQ ESSRSRRFSK LCVKNVFTVL LILIYLLLTA LAAFLAYQT ISEVLEKLKN PVMSVTYQEV DSFPRPGIAL YPGNAQLLSC SHYYHNDIPP VVEPGRPQEI DCVVTEVTYV G PFSSQGEK ...String: MRRNSYREFI DEDDEDDGNK DVPNCFDDVI DSPEEVEPND SASPDDDNRQ ESSRSRRFSK LCVKNVFTVL LILIYLLLTA LAAFLAYQT ISEVLEKLKN PVMSVTYQEV DSFPRPGIAL YPGNAQLLSC SHYYHNDIPP VVEPGRPQEI DCVVTEVTYV G PFSSQGEK RALVVRGPSE VRSKEMVFMQ FSSNETGEDF SAISYMIFAD FTDLIDSQNK SRFMGECETN CSRWTFSGGF RT WVKMSLV KTFGKQNDSV EFRQESAVVK FNDRRPAAEQ INQLYFAVFQ WRDPYIQQNK MIVTANPWSS IAILSGVFMA LFK AANFAK LTIQWIIRMR KRHLRNKERE LKQADLEDNW ETLNDNLKVI EKADNAAQVK DALTKMRAAA LDAQKATPPK LEDK SPDSP EMKDFRHGFD ILVGQIDDAL KLANEGKVKE AQAAAEQLKT TRNAYIQKYL SNSLEVLF |
-Experimental details
-Structure determination
Method | cryo EM |
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![]() | single particle reconstruction |
Aggregation state | particle |
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Sample preparation
Concentration | 1 mg/mL |
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Buffer | pH: 8 |
Vitrification | Cryogen name: ETHANE |
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Electron microscopy
Microscope | FEI TITAN KRIOS |
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Image recording | #0 - Image recording ID: 1 / #0 - Film or detector model: GATAN K2 SUMMIT (4k x 4k) / #0 - Average electron dose: 62.0 e/Å2 / #1 - Image recording ID: 2 / #1 - Film or detector model: GATAN K2 SUMMIT (4k x 4k) / #1 - Average electron dose: 62.0 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: ![]() |
Electron optics | Illumination mode: OTHER / Imaging mode: OTHER |
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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Image processing
Image recording ID | 1 |
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Final reconstruction | Resolution.type: BY AUTHOR / Resolution: 3.46 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 505115 |
Initial angle assignment | Type: ANGULAR RECONSTITUTION |
Final angle assignment | Type: ANGULAR RECONSTITUTION |