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Structure paper

TitleStructures of the TMC-1 complex illuminate mechanosensory transduction.
Journal, issue, pagesNature, Vol. 610, Issue 7933, Page 796-803, Year 2022
Publish dateOct 12, 2022
AuthorsHanbin Jeong / Sarah Clark / April Goehring / Sepehr Dehghani-Ghahnaviyeh / Ali Rasouli / Emad Tajkhorshid / Eric Gouaux /
PubMed AbstractThe 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.
External linksNature / PubMed:36224384 / PubMed Central
MethodsEM (single particle)
Resolution3.09 - 3.54 Å
Structure data

26741

7usw

EMDB-26741, PDB-7usw:
Structure of Expanded C. elegans TMC-1 complex
Method: EM (single particle) / Resolution: 3.1 Å

26742

7usx

EMDB-26742, PDB-7usx:
Structure of Contracted C. elegans TMC-1 complex
Method: EM (single particle) / Resolution: 3.09 Å

26743

7usy

EMDB-26743, PDB-7usy:
Structure of C. elegans TMC-1 complex with ARRD-6
Method: EM (single particle) / Resolution: 3.54 Å

Chemicals

ChemComp-CA:
Unknown entry

ChemComp-PEE:
1,2-dioleoyl-sn-glycero-3-phosphoethanolamine / DOPE, phospholipid*YM / Discrete optimized protein energy

ChemComp-3PE:
1,2-Distearoyl-sn-glycerophosphoethanolamine / phospholipid*YM / Phosphatidylethanolamine

ChemComp-ZFC:
undecan-1-ol / Undecanol

ChemComp-D12:
DODECANE / Dodecane

ChemComp-CLR:
CHOLESTEROL / Cholesterol

ChemComp-R16:
HEXADECANE / Hexadecane

ChemComp-NAG:
2-acetamido-2-deoxy-beta-D-glucopyranose / N-Acetylglucosamine

ChemComp-PLM:
PALMITIC ACID / Palmitic acid

Source
  • caenorhabditis elegans (invertebrata)
KeywordsMEMBRANE PROTEIN / Complex

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