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Yorodumi- EMDB-20494: Cryo-EM structure of mouse TRPV3-Y564A in putative sensitized sta... -
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Open data
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Basic information
| Entry | Database: EMDB / ID: EMD-20494 | |||||||||
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| Title | Cryo-EM structure of mouse TRPV3-Y564A in putative sensitized state at 4 degrees Celsius | |||||||||
Map data | mouse TRPV3-Y564A in putative sensitized state at 4 degrees Celsius | |||||||||
Sample |
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Keywords | Ion Channels / Membrane Protein / TRP Channels / TRANSPORT PROTEIN | |||||||||
| Function / homology | Function and homology informationnegative regulation of hair cycle / TRP channels / response to temperature stimulus / positive regulation of calcium ion import / sodium channel activity / monoatomic ion channel activity / monoatomic cation channel activity / calcium channel activity / lysosome / receptor complex ...negative regulation of hair cycle / TRP channels / response to temperature stimulus / positive regulation of calcium ion import / sodium channel activity / monoatomic ion channel activity / monoatomic cation channel activity / calcium channel activity / lysosome / receptor complex / metal ion binding / identical protein binding / membrane / plasma membrane / cytoplasm Similarity search - Function | |||||||||
| Biological species | ![]() | |||||||||
| Method | single particle reconstruction / cryo EM / Resolution: 4.07 Å | |||||||||
Authors | Singh AK / McGoldrick LL | |||||||||
| Funding support | United States, 1 items
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Citation | Journal: Nat Struct Mol Biol / Year: 2019Title: Structural basis of temperature sensation by the TRP channel TRPV3. Authors: Appu K Singh / Luke L McGoldrick / Lusine Demirkhanyan / Merfilius Leslie / Eleonora Zakharian / Alexander I Sobolevsky / ![]() Abstract: We present structures of mouse TRPV3 in temperature-dependent open, closed and intermediate states that suggest two-step activation of TRPV3 by heat. During the strongly temperature-dependent first ...We present structures of mouse TRPV3 in temperature-dependent open, closed and intermediate states that suggest two-step activation of TRPV3 by heat. During the strongly temperature-dependent first step, sensitization, the channel pore remains closed while S6 helices undergo α-to-π transitions. During the weakly temperature-dependent second step, channel opening, tight association of the S1-S4 and pore domains is stabilized by changes in the carboxy-terminal and linker domains. | |||||||||
| History |
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Structure visualization
| Movie |
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| Structure viewer | EM map: SurfView Molmil Jmol/JSmol |
| Supplemental images |
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Downloads & links
-EMDB archive
| Map data | emd_20494.map.gz | 6.3 MB | EMDB map data format | |
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| Header (meta data) | emd-20494-v30.xml emd-20494.xml | 12.4 KB 12.4 KB | Display Display | EMDB header |
| Images | emd_20494.png | 166.9 KB | ||
| Filedesc metadata | emd-20494.cif.gz | 5.6 KB | ||
| Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-20494 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-20494 | HTTPS FTP |
-Validation report
| Summary document | emd_20494_validation.pdf.gz | 436.3 KB | Display | EMDB validaton report |
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| Full document | emd_20494_full_validation.pdf.gz | 435.9 KB | Display | |
| Data in XML | emd_20494_validation.xml.gz | 5.7 KB | Display | |
| Data in CIF | emd_20494_validation.cif.gz | 6.5 KB | Display | |
| Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-20494 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-20494 | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 6pvnMC ![]() 6pvlC ![]() 6pvmC ![]() 6pvoC ![]() 6pvpC ![]() 6pvqC C: citing same article ( M: atomic model generated by this map |
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| Similar structure data |
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Links
| EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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| Related items in Molecule of the Month |
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Map
| File | Download / File: emd_20494.map.gz / Format: CCP4 / Size: 30.5 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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| Annotation | mouse TRPV3-Y564A in putative sensitized state at 4 degrees Celsius | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Voxel size | X=Y=Z: 1.06 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 : TRPV3-Y564A in putative sensitized state at 4 degree Celsius
| Entire | Name: TRPV3-Y564A in putative sensitized state at 4 degree Celsius |
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| Components |
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-Supramolecule #1: TRPV3-Y564A in putative sensitized state at 4 degree Celsius
| Supramolecule | Name: TRPV3-Y564A in putative sensitized state at 4 degree Celsius type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1 |
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| Source (natural) | Organism: ![]() |
-Macromolecule #1: Transient receptor potential cation channel subfamily V member 3
| Macromolecule | Name: Transient receptor potential cation channel subfamily V member 3 type: protein_or_peptide / ID: 1 / Number of copies: 4 / Enantiomer: LEVO |
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| Source (natural) | Organism: ![]() |
| Molecular weight | Theoretical: 92.538602 KDa |
| Recombinant expression | Organism: Homo sapiens (human) |
| Sequence | String: MNAHSKEMAP LMGKRTTAPG GNPVVLTEKR PADLTPTKKS AHFFLEIEGF EPNPTVTKTS PPIFSKPMDS NIRQCLSGNC DDMDSPQSP QDDVTETPSN PNSPSANLAK EEQRQKKKRL KKRIFAAVSE GCVEELRELL QDLQDLCRRR RGLDVPDFLM H KLTASDTG ...String: MNAHSKEMAP LMGKRTTAPG GNPVVLTEKR PADLTPTKKS AHFFLEIEGF EPNPTVTKTS PPIFSKPMDS NIRQCLSGNC DDMDSPQSP QDDVTETPSN PNSPSANLAK EEQRQKKKRL KKRIFAAVSE GCVEELRELL QDLQDLCRRR RGLDVPDFLM H KLTASDTG KTCLMKALLN INPNTKEIVR ILLAFAEEND ILDRFINAEY TEEAYEGQTA LNIAIERRQG DITAVLIAAG AD VNAHAKG VFFNPKYQHE GFYFGETPLA LAACTNQPEI VQLLMENEQT DITSQDSRGN NILHALVTVA EDFKTQNDFV KRM YDMILL RSGNWELETM RNNDGLTPLQ LAAKMGKAEI LKYILSREIK EKPLRSLSRK FTDWAYGPVS SSLYDLTNVD TTTD NSVLE IIVYNTNIDN RHEMLTLEPL HTLLHTKWKK FAKYMFFLSF CFYFFYNITL TLVSYYRPRE DEDLPHPLAL THKMS WLQL LGRMFVLIWA TCISVKEGIA IFLLRPSDLQ SILSDAWFHF VFFVQAVLVI LSVFLYLFAY KEYLACLVLA MALGWA NML AYTRGFQSMG MYSVMIQKVI LHDVLKFLFV YILFLLGFGV ALASLIEKCS KDKKDCSSYG SFSDAVLELF KLTIGLG DL NIQQNSTYPI LFLFLLITYV ILTFVLLLNM LIALMGETVE NVSKESERIW RLQRARTILE FEKMLPEWLR SRFRMGEL C KVADEDFRLC LRINEVKWTE WKTHVSFLNE DPGPIRRTAD LNKIQDSSRS NSKTTLYAFD ELDEFPETSV LVPRGSAAA WSHPQFEK UniProtKB: Transient receptor potential cation channel subfamily V member 3 |
-Macromolecule #2: SODIUM ION
| Macromolecule | Name: SODIUM ION / type: ligand / ID: 2 / Number of copies: 2 |
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| Molecular weight | Theoretical: 22.99 Da |
-Experimental details
-Structure determination
| Method | cryo EM |
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Processing | single particle reconstruction |
| Aggregation state | particle |
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Sample preparation
| Concentration | 4.07 mg/mL |
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| Buffer | pH: 8 Details: 150 mM NaCl, 20 mM Tris-HCl, pH 8.0, 1 mM BME, 0.01% GDN |
| Grid | Support film - Material: CARBON / Support film - topology: HOLEY / Details: unspecified |
| Vitrification | Cryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 42 K / Instrument: FEI VITROBOT MARK IV |
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Electron microscopy
| Microscope | FEI TITAN KRIOS |
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| Image recording | Film or detector model: GATAN K2 SUMMIT (4k x 4k) / Detector mode: COUNTING / Average electron dose: 57.0 e/Å2 |
| Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
| Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD |
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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Image processing
| Startup model | Type of model: PDB ENTRY PDB model - PDB ID: |
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| Final reconstruction | Resolution.type: BY AUTHOR / Resolution: 4.07 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: RELION / Number images used: 130958 |
| Initial angle assignment | Type: PROJECTION MATCHING |
| Final angle assignment | Type: PROJECTION MATCHING |
-Atomic model buiding 1
| Refinement | Space: REAL / Protocol: FLEXIBLE FIT |
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| Output model | ![]() PDB-6pvn: |
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About Yorodumi


Keywords
Authors
United States, 1 items
Citation
UCSF Chimera



















Z (Sec.)
Y (Row.)
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Homo sapiens (human)

