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Open data
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Basic information
Entry | Database: PDB / ID: 7usw | ||||||||||||
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Title | Structure of Expanded C. elegans TMC-1 complex | ||||||||||||
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![]() | MEMBRANE PROTEIN / Complex | ||||||||||||
Function / homology | ![]() detection of stimulus involved in sensory perception / striated muscle dense body / sensory perception of chemical stimulus / mechanosensitive monoatomic ion channel activity / non-motile cilium / sodium channel activity / calcium ion homeostasis / monoatomic ion transmembrane transport / monoatomic ion channel activity / neuronal cell body ...detection of stimulus involved in sensory perception / striated muscle dense body / sensory perception of chemical stimulus / mechanosensitive monoatomic ion channel activity / non-motile cilium / sodium channel activity / calcium ion homeostasis / monoatomic ion transmembrane transport / monoatomic ion channel activity / neuronal cell body / calcium ion binding / magnesium ion binding / membrane / plasma membrane / cytoplasm Similarity search - Function | ||||||||||||
Biological species | ![]() ![]() | ||||||||||||
Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.1 Å | ||||||||||||
![]() | Jeong, H. / Clark, S. / Gouaux, E. | ||||||||||||
Funding support | ![]()
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![]() | ![]() Title: Structures of the TMC-1 complex illuminate mechanosensory transduction. Authors: Hanbin Jeong / Sarah Clark / April Goehring / Sepehr Dehghani-Ghahnaviyeh / Ali Rasouli / Emad Tajkhorshid / Eric Gouaux / ![]() Abstract: The initial step in the sensory transduction pathway underpinning hearing and balance in mammals involves the conversion of force into the gating of a mechanosensory transduction channel. Despite the ...The initial step in the sensory transduction pathway underpinning hearing and balance in mammals involves the conversion of force into the gating of a mechanosensory transduction channel. Despite the profound socioeconomic impacts of hearing disorders and the fundamental biological significance of understanding mechanosensory transduction, the composition, structure and mechanism of the mechanosensory transduction complex have remained poorly characterized. Here we report the single-particle cryo-electron microscopy structure of the native transmembrane channel-like protein 1 (TMC-1) mechanosensory transduction complex isolated from Caenorhabditis elegans. The two-fold symmetric complex is composed of two copies each of the pore-forming TMC-1 subunit, the calcium-binding protein CALM-1 and the transmembrane inner ear protein TMIE. CALM-1 makes extensive contacts with the cytoplasmic face of the TMC-1 subunits, whereas the single-pass TMIE subunits reside on the periphery of the complex, poised like the handles of an accordion. A subset of complexes additionally includes a single arrestin-like protein, arrestin domain protein (ARRD-6), bound to a CALM-1 subunit. Single-particle reconstructions and molecular dynamics simulations show how the mechanosensory transduction complex deforms the membrane bilayer and suggest crucial roles for lipid-protein interactions in the mechanism by which mechanical force is transduced to ion channel gating. | ||||||||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 382.3 KB | Display | ![]() |
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PDB format | ![]() | 299.5 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 2.3 MB | Display | ![]() |
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Full document | ![]() | 2.4 MB | Display | |
Data in XML | ![]() | 62.9 KB | Display | |
Data in CIF | ![]() | 87.5 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 26741MC ![]() 7usxC ![]() 7usyC M: map data used to model this data C: citing same article ( |
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Similar structure data | Similarity search - Function & homology ![]() |
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Links
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Assembly
Deposited unit | ![]()
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1 |
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Components
-Transmembrane ... , 2 types, 4 molecules ABDF
#1: Protein | Mass: 147331.812 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() #3: Protein | Mass: 12668.813 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() |
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-Protein / Sugars , 2 types, 4 molecules CE![](data/chem/img/NAG.gif)
![](data/chem/img/NAG.gif)
#11: Sugar | #2: Protein | Mass: 23568.568 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() |
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-Non-polymers , 8 types, 68 molecules ![](data/chem/img/CA.gif)
![](data/chem/img/PEE.gif)
![](data/chem/img/3PE.gif)
![](data/chem/img/ZFC.gif)
![](data/chem/img/D12.gif)
![](data/chem/img/CLR.gif)
![](data/chem/img/R16.gif)
![](data/chem/img/PLM.gif)
![](data/chem/img/PEE.gif)
![](data/chem/img/3PE.gif)
![](data/chem/img/ZFC.gif)
![](data/chem/img/D12.gif)
![](data/chem/img/CLR.gif)
![](data/chem/img/R16.gif)
![](data/chem/img/PLM.gif)
#4: Chemical | ChemComp-CA / #5: Chemical | #6: Chemical | #7: Chemical | ChemComp-ZFC / #8: Chemical | ChemComp-D12 / #9: Chemical | #10: Chemical | ChemComp-R16 / #12: Chemical | ChemComp-PLM / |
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-Details
Has ligand of interest | Y |
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-Experimental details
-Experiment
Experiment | Method: ELECTRON MICROSCOPY |
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EM experiment | Aggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction |
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Sample preparation
Component | Name: Native TMC-1 complex / Type: COMPLEX / Entity ID: #1-#3 / Source: NATURAL |
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Molecular weight | Value: 0.43 MDa / Experimental value: YES |
Source (natural) | Organism: ![]() ![]() |
Buffer solution | pH: 8.5 |
Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES |
Vitrification | Cryogen name: ETHANE |
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Electron microscopy imaging
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company | ||||||||||||
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Microscopy | Model: FEI TITAN KRIOS | ||||||||||||
Electron gun | Electron source: ![]() | ||||||||||||
Electron lens | Mode: BRIGHT FIELD / Nominal defocus max: 2400 nm / Nominal defocus min: 1000 nm | ||||||||||||
Image recording |
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Processing
Image processing |
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CTF correction |
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3D reconstruction |
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Refinement | Highest resolution: 3.1 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints |
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