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Open data
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Basic information
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Title | cryo-EM structure of human TMEM63A | |||||||||
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![]() | mechanically activated (MA) ion channel / ![]() | |||||||||
Function / homology | ![]() osmolarity-sensing monoatomic cation channel activity / mechanosensitive monoatomic ion channel activity / calcium-activated cation channel activity / tertiary granule membrane / centriolar satellite / specific granule membrane / ![]() ![]() ![]() Similarity search - Function | |||||||||
Biological species | ![]() ![]() | |||||||||
Method | ![]() ![]() | |||||||||
![]() | Yang D | |||||||||
Funding support | ![]()
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![]() | ![]() Title: A monomeric structure of human TMEM63A protein. Authors: Xuening Wu / Tiantian Shang / Xinyi Lü / Deyi Luo / Dongxue Yang / ![]() Abstract: OSCA/TMEM63 is a newly identified family of mechanically activated (MA) ion channels in plants and animals, respectively, which convert physical forces into electrical signals or trigger ...OSCA/TMEM63 is a newly identified family of mechanically activated (MA) ion channels in plants and animals, respectively, which convert physical forces into electrical signals or trigger intracellular cascades and are essential for eukaryotic physiology. OSCAs and related TMEM16s and transmembrane channel-like (TMC) proteins form homodimers with two pores. However, the molecular architecture of the mammalian TMEM63 proteins remains unclear. Here we elucidate the structure of human TMEM63A in the presence of calcium by single particle cryo-EM, revealing a distinct monomeric architecture containing eleven transmembrane helices. It has structural similarity to the single subunit of the Arabidopsis thaliana OSCA proteins. We locate the ion permeation pathway within the monomeric configuration and observe a nonprotein density resembling lipid. These results lay a foundation for understanding the structural organization of OSCA/TMEM63A family proteins. | |||||||||
History |
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Structure visualization
Supplemental images |
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Downloads & links
-EMDB archive
Map data | ![]() | 59.6 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 15.6 KB 15.6 KB | Display Display | ![]() |
Images | ![]() | 100.4 KB | ||
Filedesc metadata | ![]() | 5.4 KB | ||
Others | ![]() ![]() ![]() | 31.8 MB 59.4 MB 59.4 MB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 8wuaMC M: atomic model generated by this map C: citing same article ( |
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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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Annotation | sharpen map | ||||||||||||||||||||
Voxel size | X=Y=Z: 1.0979 Å | ||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
-Additional map: unsharpen map
File | emd_37852_additional_1.map | ||||||||||||
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Annotation | unsharpen map | ||||||||||||
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Density Histograms |
-Half map: half map A
File | emd_37852_half_map_1.map | ||||||||||||
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Annotation | half map A | ||||||||||||
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Density Histograms |
-Half map: half map B
File | emd_37852_half_map_2.map | ||||||||||||
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Annotation | half map B | ||||||||||||
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Sample components
-Entire : human TMEM63A
Entire | Name: human TMEM63A |
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Components |
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-Supramolecule #1: human TMEM63A
Supramolecule | Name: human TMEM63A / type: complex / ID: 1 / Parent: 0 / Macromolecule list: all |
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Source (natural) | Organism: ![]() ![]() |
-Macromolecule #1: CSC1-like protein 1
Macromolecule | Name: CSC1-like protein 1 / type: protein_or_peptide / ID: 1 / Number of copies: 1 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() ![]() |
Molecular weight | Theoretical: 82.331828 KDa |
Recombinant expression | Organism: ![]() ![]() |
Sequence | String: FLELWQSKAV SIREQLGLGD RPNDSYCYNS AKNSTVLQGV TFGGIPTVLL IDVSCFLFLI LVFSIIRRRF WDYGRIALVS EADSESRFQ RLSSTSSSGQ QDFENELGCC PWLTAIFRLH DDQILEWCGE DAIHYLSFQR HIIFLLVVVS FLSLCVILPV N LSGDLLDK ...String: FLELWQSKAV SIREQLGLGD RPNDSYCYNS AKNSTVLQGV TFGGIPTVLL IDVSCFLFLI LVFSIIRRRF WDYGRIALVS EADSESRFQ RLSSTSSSGQ QDFENELGCC PWLTAIFRLH DDQILEWCGE DAIHYLSFQR HIIFLLVVVS FLSLCVILPV N LSGDLLDK DPYSFGRTTI ANLQTDNDLL WLHTIFAVIY LFLTVGFMRH HTQSIKYKEE NLVRRTLFIT GLPRDARKET VE SHFRDAY PTCEVVDVQL CYNVAKLIYL CKEKKKTEKS LTYYTNLQVK TGQRTLINPK PCGQFCCCEV LGCEWEDAIS YYT RMKDRL LERITEEERH VQDQPLGMAF VTFQEKSMAT YILKDFNACK CQSLQCKGEP QPSSHSRELY TSKWTVTFAA DPED ICWKN LSIQGLRWWL QWLGINFTLF LGLFFLTTPS IILSTMDKFN VTKPIHALNN PIISQFFPTL LLWSFSALLP SIVYY STLL ESHWTKSGEN QIMMTKVYIF LIFMVLILPS LGLTSLDFFF RWLFDKTSSE ASIRLECVFL PDQGAFFVNY VIASAF IGN GMELLRLPGL ILYTFRMIMA KTAADRRNVK QNQAFQYEFG AMYAWMLCVF TVIVAYSITC PIIAPFGLIY ILLKHMV DR HNLYFVYLPA KLEKGIHFAA VNQALAAPIL CLFWLYFFSF LRLGMKAPAT LFTFLVLLLT ILVCLAHTCF GC UniProtKB: CSC1-like protein 1 |
-Experimental details
-Structure determination
Method | ![]() |
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Aggregation state | particle |
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Sample preparation
Buffer | pH: 8 |
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Vitrification | Cryogen name: ETHANE |
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Electron microscopy
Microscope | FEI TITAN KRIOS |
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Electron beam | Acceleration voltage: 300 kV / Electron source: ![]() |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD![]() |
Image recording | Film or detector model: GATAN K3 (6k x 4k) / Average electron dose: 1.56 e/Å2 |
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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Image processing
Startup model | Type of model: OTHER / Details: Ab initio |
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Initial angle assignment | Type: MAXIMUM LIKELIHOOD |
Final angle assignment | Type: MAXIMUM LIKELIHOOD |
Final reconstruction | Resolution.type: BY AUTHOR / Resolution: 3.6 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 163395 |