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- EMDB-20498: Cryo-EM Structure of Thermo-Sensitive TRP Channel TRP1 from the A... -
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Open data
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Basic information
Entry | Database: EMDB / ID: EMD-20498 | |||||||||
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Title | Cryo-EM Structure of Thermo-Sensitive TRP Channel TRP1 from the Alga Chlamydomonas reinhardtii in Detergent | |||||||||
![]() | Thermo-Sensitive TRP Channel TRP1 from the Alga Chlamydomonas reinhardtii in detergent | |||||||||
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![]() | Ion Channels / Membrane Protein / TRP Channels / TRANSPORT PROTEIN | |||||||||
Function / homology | ![]() store-operated calcium channel activity / cation channel complex / inositol 1,4,5 trisphosphate binding / regulation of cytosolic calcium ion concentration / calcium ion transmembrane transport / plasma membrane Similarity search - Function | |||||||||
Biological species | ![]() ![]() | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 3.53 Å | |||||||||
![]() | McGoldrick LL / Singh AK | |||||||||
Funding support | ![]()
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![]() | ![]() Title: Structure of the thermo-sensitive TRP channel TRP1 from the alga Chlamydomonas reinhardtii. Authors: Luke L McGoldrick / Appu K Singh / Lusine Demirkhanyan / Ting-Yu Lin / Ryan G Casner / Eleonora Zakharian / Alexander I Sobolevsky / ![]() Abstract: Algae produce the largest amount of oxygen on earth and are invaluable for human nutrition and biomedicine, as well as for the chemical industry, energy production and agriculture. The mechanisms by ...Algae produce the largest amount of oxygen on earth and are invaluable for human nutrition and biomedicine, as well as for the chemical industry, energy production and agriculture. The mechanisms by which algae can detect and respond to changes in their environments can rely on membrane receptors, including TRP ion channels. Here we present a 3.5-Å resolution cryo-EM structure of the transient receptor potential (TRP) channel crTRP1 from the alga Chlamydomonas reinhardtii that opens in response to increased temperature and is positively regulated by the membrane lipid PIP. The structure of crTRP1 significantly deviates from the structures of other TRP channels and has a unique 2-fold symmetrical rose-shape architecture with elbow domains and ankyrin repeat domains submerged and dipping into the membrane, respectively. Our study provides a structure of a TRP channel from a micro-organism and a structural framework for better understanding algae biology and TRP channel evolution. | |||||||||
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 | ![]() | 4.8 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 12.9 KB 12.9 KB | Display Display | ![]() |
Images | ![]() | 191.2 KB | ||
Filedesc metadata | ![]() | 6.2 KB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Validation report
Summary document | ![]() | 437.2 KB | Display | ![]() |
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Full document | ![]() | 436.8 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 | ![]() 6pw4MC ![]() 6pw5C 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 | ![]() ![]() |
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Related items in Molecule of the Month |
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Map
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Annotation | Thermo-Sensitive TRP Channel TRP1 from the Alga Chlamydomonas reinhardtii in detergent | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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 : crTRP1 in detergent
Entire | Name: crTRP1 in detergent |
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Components |
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-Supramolecule #1: crTRP1 in detergent
Supramolecule | Name: crTRP1 in detergent / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1 |
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Source (natural) | Organism: ![]() ![]() |
-Macromolecule #1: TRP-like ion channel
Macromolecule | Name: TRP-like ion channel / type: protein_or_peptide / ID: 1 / Number of copies: 4 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() ![]() |
Molecular weight | Theoretical: 99.538742 KDa |
Recombinant expression | Organism: ![]() |
Sequence | String: MKVAPAPASG QPGGGSKKPS DYGCQLHYKH ARVVEPESTT DDGMKRLKDV GDKGTLITAA ELGLVDKYRD LKRAGQDILT CDWPYHYSS ILYACYGNQY KILQMVEREF VGSTQELTAM HTTRCWVGKN SAMVAAYQGH LETMLYIIDL DMQGKFTEDL F KQRDVMGK ...String: MKVAPAPASG QPGGGSKKPS DYGCQLHYKH ARVVEPESTT DDGMKRLKDV GDKGTLITAA ELGLVDKYRD LKRAGQDILT CDWPYHYSS ILYACYGNQY KILQMVEREF VGSTQELTAM HTTRCWVGKN SAMVAAYQGH LETMLYIIDL DMQGKFTEDL F KQRDVMGK NAMMWAASQG HTDTIEVLLV RSLYRLLPED CADPLVLKTR WKLVSLLADL ASHCRDYDPG CSRSFFQEVL AS IKYDPVE GARQEEAAAA GGGGSAREGA ALHEPTWGVD DGEEEERRHG VKHSDLVGKS AASTTAAAAA GGKTASGKPG EPG GGGAVK LKDVHITVRT LQGVIVSAYR AGMNCMGVIM YCQSLLQQAR YFDDLVAQLT AWEVKLLDTC RNKQEVQAIL APTE DDPSE PVGYALATFD KAFLSHKFVQ QIFTEKWDTM GVTDYTKSLF GVVWGGCSLV VAFAAWATIC PLVVVARSFL SPVQD FMMR GKVIVDSRFP WHVPLYRWLL TQCALITFTV LLSYLVFSFD PSDPVPASVA PLNTFLAVWC AAILVDEVQE YVEEGR AEY MSSGWNVMDV TMALSYILHY ILRIIAVRVT DNLNILLVVN DLLAAAALMA WFRMVSVFEL SSAIGPLIQM MKQMLIK DV TRFALLVLVI LLGFSVGMEA LFQEACIERD PTTNECTKYT SWGYDWQKDG LVGGMTFLQY IALGNANPVD FEQKRVTG V IFYLIFAIVT AILLLNLFIA MLADTYTRVS TQAMVEFRYR KAKLMASYSR RDFVCPPFNL LHLVCAAVGN GLRRLVWGP DGFTPVSMRK NETVPLFSWY FPQGEEMRQV VVLQRRVVDD FLNSNRVALF REKLNAELPN LVHEMLKQKG KGDGGALAGG GAAASTTVL ATAVSVTAAA GH UniProtKB: TRP-like ion channel |
-Macromolecule #2: [(2R)-2-octanoyloxy-3-[oxidanyl-[(1R,2R,3S,4R,5R,6S)-2,3,6-tris(o...
Macromolecule | Name: [(2R)-2-octanoyloxy-3-[oxidanyl-[(1R,2R,3S,4R,5R,6S)-2,3,6-tris(oxidanyl)-4,5-diphosphonooxy-cyclohexyl]oxy-phosphoryl]oxy-propyl] octanoate type: ligand / ID: 2 / Number of copies: 2 / Formula: PIO |
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Molecular weight | Theoretical: 746.566 Da |
Chemical component information | ![]() ChemComp-PIO: |
-Macromolecule #3: 1,2-DIOLEOYL-SN-GLYCERO-3-PHOSPHOCHOLINE
Macromolecule | Name: 1,2-DIOLEOYL-SN-GLYCERO-3-PHOSPHOCHOLINE / type: ligand / ID: 3 / Number of copies: 2 / Formula: PCW |
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Molecular weight | Theoretical: 787.121 Da |
Chemical component information | ![]() ChemComp-PCW: |
-Macromolecule #4: 1-PALMITOYL-2-LINOLEOYL-SN-GLYCERO-3-PHOSPHOCHOLINE
Macromolecule | Name: 1-PALMITOYL-2-LINOLEOYL-SN-GLYCERO-3-PHOSPHOCHOLINE / type: ligand / ID: 4 / Number of copies: 2 / Formula: CPL |
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Molecular weight | Theoretical: 758.06 Da |
Chemical component information | ![]() ChemComp-CPL: |
-Macromolecule #5: (2S)-3-{[(R)-hydroxy{[(1R,2R,3S,4R,5R,6S)-2,3,6-trihydroxy-4,5-bi...
Macromolecule | Name: (2S)-3-{[(R)-hydroxy{[(1R,2R,3S,4R,5R,6S)-2,3,6-trihydroxy-4,5-bis(phosphonooxy)cyclohexyl]oxy}phosphoryl]oxy}propane-1,2-diyl dihexadecanoate type: ligand / ID: 5 / Number of copies: 4 / Formula: PIK |
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Molecular weight | Theoretical: 970.992 Da |
Chemical component information | ![]() ChemComp-PIK: |
-Experimental details
-Structure determination
Method | cryo EM |
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![]() | single particle reconstruction |
Aggregation state | particle |
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Sample preparation
Concentration | 2 mg/mL |
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Buffer | pH: 8 Details: 150 mM NaCl, 20 mM Tris-HCl pH 8.0, 1 mM BME and 0.01% GDN |
Grid | Support film - Material: CARBON / Support film - topology: HOLEY / Details: unspecified |
Vitrification | Cryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 277 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: 61.0 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: ![]() |
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: NONE |
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Final reconstruction | Applied symmetry - Point group: C2 (2 fold cyclic) / Resolution.type: BY AUTHOR / Resolution: 3.53 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 63018 |
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-6pw4: |