+Open data
-Basic information
Entry | Database: PDB / ID: 8tkp | ||||||
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Title | Structure of the C. elegans TMC-2 complex | ||||||
Components |
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Keywords | MEMBRANE PROTEIN / Mechanosensory transduction Macromolecular complex | ||||||
Function / homology | Function and homology information striated muscle dense body / mechanosensitive monoatomic ion channel activity / calcium ion homeostasis / calcium ion binding / magnesium ion binding / membrane / plasma membrane / cytoplasm Similarity search - Function | ||||||
Biological species | Caenorhabditis elegans (invertebrata) | ||||||
Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 2.9 Å | ||||||
Authors | Clark, S. / Jeong, H. / Goehring, A. / Posert, R. / Gouaux, E. | ||||||
Funding support | United States, 1items
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Citation | Journal: Proc Natl Acad Sci U S A / Year: 2024 Title: The structure of the TMC-2 complex suggests roles of lipid-mediated subunit contacts in mechanosensory transduction. Authors: Sarah Clark / Hanbin Jeong / Rich Posert / April Goehring / Eric Gouaux / Abstract: Mechanotransduction is the process by which a mechanical force, such as touch, is converted into an electrical signal. Transmembrane channel-like (TMC) proteins are an evolutionarily conserved family ...Mechanotransduction is the process by which a mechanical force, such as touch, is converted into an electrical signal. Transmembrane channel-like (TMC) proteins are an evolutionarily conserved family of membrane proteins whose function has been linked to a variety of mechanosensory processes, including hearing and balance sensation in vertebrates and locomotion in . TMC1 and TMC2 are components of ion channel complexes, but the molecular features that tune these complexes to diverse mechanical stimuli are unknown. express two TMC homologs, TMC-1 and TMC-2, both of which are the likely pore-forming subunits of mechanosensitive ion channels but differ in their expression pattern and functional role in the worm. Here, we present the single-particle cryo-electron microscopy structure of the native TMC-2 complex isolated from . The complex is composed of two copies of the pore-forming TMC-2 subunit, the calcium and integrin binding protein CALM-1 and the transmembrane inner ear protein TMIE. Comparison of the TMC-2 complex to the recently published cryo-EM structure of the TMC-1 complex highlights conserved protein-lipid interactions, as well as a π-helical structural motif in the pore-forming helices, that together suggest a mechanism for TMC-mediated mechanosensory transduction. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 8tkp.cif.gz | 369.6 KB | Display | PDBx/mmCIF format |
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PDB format | pdb8tkp.ent.gz | 286.5 KB | Display | PDB format |
PDBx/mmJSON format | 8tkp.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 8tkp_validation.pdf.gz | 2.2 MB | Display | wwPDB validaton report |
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Full document | 8tkp_full_validation.pdf.gz | 2.2 MB | Display | |
Data in XML | 8tkp_validation.xml.gz | 72.7 KB | Display | |
Data in CIF | 8tkp_validation.cif.gz | 103.4 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/tk/8tkp ftp://data.pdbj.org/pub/pdb/validation_reports/tk/8tkp | HTTPS FTP |
-Related structure data
Related structure data | 41356MC 41432 M: map data used to model this data C: citing same article (ref.) |
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Similar structure data | Similarity search - Function & homologyF&H Search |
-Links
-Assembly
Deposited unit |
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1 |
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-Components
-Transmembrane ... , 2 types, 4 molecules ADCF
#1: Protein | Mass: 136232.609 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Caenorhabditis elegans (invertebrata) / Gene: tmc-2, B0416.1 / Production host: Caenorhabditis elegans (invertebrata) / References: UniProt: Q11069 #3: Protein | Mass: 12668.813 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Caenorhabditis elegans (invertebrata) / Gene: CELE_Y39A1C.1, Y39A1C.1 / Production host: Caenorhabditis elegans (invertebrata) / References: UniProt: Q9XXE7 |
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-Protein , 1 types, 2 molecules BE
#2: Protein | Mass: 23568.568 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Caenorhabditis elegans (invertebrata) / Gene: calm-1, CELE_F30A10.1, F30A10.1 / Production host: Caenorhabditis elegans (invertebrata) / References: UniProt: Q93640 |
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-Sugars , 3 types, 4 molecules
#4: Polysaccharide | 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-3)-2-acetamido-2-deoxy-beta-D-glucopyranose Source method: isolated from a genetically manipulated source |
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#5: Polysaccharide | 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose Source method: isolated from a genetically manipulated source |
#10: Sugar |
-Non-polymers , 6 types, 48 molecules
#6: Chemical | ChemComp-TWT / #7: Chemical | ChemComp-PEE / #8: Chemical | ChemComp-R16 / #9: Chemical | #11: Chemical | ChemComp-CA / #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: TISSUE / 3D reconstruction method: single particle reconstruction |
-Sample preparation
Component | Name: C. elegans TMC-2 complex / Type: COMPLEX / Entity ID: #1-#3 / Source: NATURAL |
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Source (natural) | Organism: Caenorhabditis elegans (invertebrata) |
Buffer solution | pH: 8 / Details: 50 mM Tris pH 8.0, 150 mM NaCl, 0.02% GDN |
Specimen | Conc.: 0.003 mg/ml / Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES Details: Native TMC-2 complex, isolated from transgenic C. elegans. |
Specimen support | Grid material: GOLD / Grid mesh size: 300 divisions/in. / Grid type: Quantifoil R2/1 |
Vitrification | Instrument: FEI VITROBOT MARK IV / Cryogen name: ETHANE / Humidity: 100 % / Chamber temperature: 283 K |
-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: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM |
Electron lens | Mode: BRIGHT FIELD / Nominal defocus max: 2500 nm / Nominal defocus min: 1500 nm / Cs: 2.7 mm |
Image recording | Electron dose: 50 e/Å2 / Film or detector model: GATAN K3 BIOQUANTUM (6k x 4k) |
-Processing
EM software |
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CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION | |||||||||
3D reconstruction | Resolution: 2.9 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 207726 / Symmetry type: POINT |