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TitleThe conformational cycle of prestin underlies outer-hair cell electromotility.
Journal, issue, pagesNature, Vol. 600, Issue 7889, Page 553-558, Year 2021
Publish dateOct 25, 2021
AuthorsNavid Bavi / Michael David Clark / Gustavo F Contreras / Rong Shen / Bharat G Reddy / Wieslawa Milewski / Eduardo Perozo /
PubMed AbstractThe voltage-dependent motor protein prestin (also known as SLC26A5) is responsible for the electromotive behaviour of outer-hair cells and underlies the cochlear amplifier. Knockout or impairment of ...The voltage-dependent motor protein prestin (also known as SLC26A5) is responsible for the electromotive behaviour of outer-hair cells and underlies the cochlear amplifier. Knockout or impairment of prestin causes severe hearing loss. Despite the key role of prestin in hearing, the mechanism by which mammalian prestin senses voltage and transduces it into cellular-scale movements (electromotility) is poorly understood. Here we determined the structure of dolphin prestin in six distinct states using single-particle cryo-electron microscopy. Our structural and functional data suggest that prestin adopts a unique and complex set of states, tunable by the identity of bound anions (Cl or SO). Salicylate, a drug that can cause reversible hearing loss, competes for the anion-binding site of prestin, and inhibits its function by immobilizing prestin in a new conformation. Our data suggest that the bound anion together with its coordinating charged residues and helical dipole act as a dynamic voltage sensor. An analysis of all of the anion-dependent conformations reveals how structural rearrangements in the voltage sensor are coupled to conformational transitions at the protein-membrane interface, suggesting a previously undescribed mechanism of area expansion. Visualization of the electromotility cycle of prestin distinguishes the protein from the closely related SLC26 anion transporters, highlighting the basis for evolutionary specialization of the mammalian cochlear amplifier at a high resolution.
External linksNature / PubMed:34695838
MethodsEM (single particle)
Resolution3.3 - 6.7 Å
Structure data

24928

7s8x

EMDB-24928, PDB-7s8x:
Cryo-EM Structure of dolphin Prestin: Sensor Up (compact) state
Method: EM (single particle) / Resolution: 3.3 Å

24930

7s9a

EMDB-24930, PDB-7s9a:
Cryo-EM Structure of dolphin Prestin: Inhibited I (Chloride + Salicylate)
Method: EM (single particle) / Resolution: 3.8 Å

24931

7s9b

EMDB-24931, PDB-7s9b:
Cryo-EM Structure of dolphin Prestin: Sensor Down I (Expanded) state
Method: EM (single particle) / Resolution: 4.2 Å

24932

7s9c

EMDB-24932, PDB-7s9c:
Cryo-EM Structure of dolphin Prestin: Sensor Down II (Expanded II) state
Method: EM (single particle) / Resolution: 6.7 Å

24933

7s9d

EMDB-24933, PDB-7s9d:
Cryo-EM Structure of dolphin Prestin: Intermediate state
Method: EM (single particle) / Resolution: 4.6 Å

24934

7s9e

EMDB-24934, PDB-7s9e:
Cryo-EM Structure of dolphin Prestin: Inhibited II (Sulfate +Salicylate) state
Method: EM (single particle) / Resolution: 3.7 Å

Chemicals

ChemComp-SAL:
2-HYDROXYBENZOIC ACID / Salicylic acid

Source
  • tursiops truncatus (common bottlenose dolphin)
KeywordsMOTOR PROTEIN / Outer hair cells / electromotility / mechanotransduction / hearing / deafness / frequency sensation / echolocation / SLC26 / SLC26A5

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