Single particle cryo-EM structure of the outer hair cell motor protein prestin

Carmen Butan, Qiang Song, Jun-Ping Bai, Winston J. T. Tan, Dhasakumar Navaratnam () and Joseph Santos-Sacchi ()
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Carmen Butan: Yale University School of Medicine
Qiang Song: Yale University School of Medicine
Jun-Ping Bai: Yale University School of Medicine
Winston J. T. Tan: Yale University School of Medicine
Dhasakumar Navaratnam: Yale University School of Medicine
Joseph Santos-Sacchi: Yale University School of Medicine

Nature Communications, 2022, vol. 13, issue 1, 1-11

Abstract: Abstract The mammalian outer hair cell (OHC) protein prestin (Slc26a5) differs from other Slc26 family members due to its unique piezoelectric-like property that drives OHC electromotility, the putative mechanism for cochlear amplification. Here, we use cryo-electron microscopy to determine prestin’s structure at 3.6 Å resolution. Prestin is structurally similar to the anion transporter Slc26a9. It is captured in an inward-open state which may reflect prestin’s contracted state. Two well-separated transmembrane (TM) domains and two cytoplasmic sulfate transporter and anti-sigma factor antagonist (STAS) domains form a swapped dimer. The transmembrane domains consist of 14 transmembrane segments organized in two 7+7 inverted repeats, an architecture first observed in the bacterial symporter UraA. Mutation of prestin’s chloride binding site removes salicylate competition with anions while retaining the prestin characteristic displacement currents (Nonlinear Capacitance), undermining the extrinsic voltage sensor hypothesis for prestin function.

Date: 2022
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DOI: 10.1038/s41467-021-27915-z

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