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

Author

Listed:
  • 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
    Yale University School of Medicine
    Yale University School of Medicine)

  • Joseph Santos-Sacchi

    (Yale University School of Medicine
    Yale University School of Medicine
    Yale University School of Medicine)

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.

Suggested Citation

  • Carmen Butan & Qiang Song & Jun-Ping Bai & Winston J. T. Tan & Dhasakumar Navaratnam & Joseph Santos-Sacchi, 2022. "Single particle cryo-EM structure of the outer hair cell motor protein prestin," Nature Communications, Nature, vol. 13(1), pages 1-11, December.
    • Handle: RePEc:nat:natcom:v:13:y:2022:i:1:d:10.1038_s41467-021-27915-z
    DOI: 10.1038/s41467-021-27915-z
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    Cited by:

    1. Qianying Liu & Xiang Zhang & Hui Huang & Yuxin Chen & Fang Wang & Aihua Hao & Wuqiang Zhan & Qiyu Mao & Yuxia Hu & Lin Han & Yifang Sun & Meng Zhang & Zhimin Liu & Geng-Lin Li & Weijia Zhang & Yilai S, 2023. "Asymmetric pendrin homodimer reveals its molecular mechanism as anion exchanger," Nature Communications, Nature, vol. 14(1), pages 1-11, December.
    2. Benedikt T. Kuhn & Jonathan Zöller & Iwan Zimmermann & Tim Gemeinhardt & Dogukan H. Özkul & Julian D. Langer & Markus A. Seeger & Eric R. Geertsma, 2024. "Interdomain-linkers control conformational transitions in the SLC23 elevator transporter UraA," Nature Communications, Nature, vol. 15(1), pages 1-12, December.
    3. Haon Futamata & Masahiro Fukuda & Rie Umeda & Keitaro Yamashita & Atsuhiro Tomita & Satoe Takahashi & Takafumi Shikakura & Shigehiko Hayashi & Tsukasa Kusakizako & Tomohiro Nishizawa & Kazuaki Homma &, 2022. "Cryo-EM structures of thermostabilized prestin provide mechanistic insights underlying outer hair cell electromotility," Nature Communications, Nature, vol. 13(1), pages 1-14, December.
    4. Wenxin Hu & Alex Song & Hongjin Zheng, 2024. "Substrate binding plasticity revealed by Cryo-EM structures of SLC26A2," Nature Communications, Nature, vol. 15(1), pages 1-9, December.

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