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Cryo-EM structure of the sodium-driven chloride/bicarbonate exchanger NDCBE

Author

Listed:
  • Weiguang Wang

    (University of California
    California NanoSystems Institute, University of California)

  • Kirill Tsirulnikov

    (University of California)

  • Hristina R. Zhekova

    (University of Calgary)

  • Gülru Kayık

    (University of Calgary)

  • Hanif Muhammad Khan

    (University of Calgary)

  • Rustam Azimov

    (University of California)

  • Natalia Abuladze

    (University of California)

  • Liyo Kao

    (University of California)

  • Debbie Newman

    (University of California)

  • Sergei Yu. Noskov

    (University of Calgary)

  • Z. Hong Zhou

    (California NanoSystems Institute, University of California
    University of California)

  • Alexander Pushkin

    (University of California)

  • Ira Kurtz

    (University of California
    Brain Research Institute, University of California)

Abstract

SLC4 transporters play significant roles in pH regulation and cellular sodium transport. The previously solved structures of the outward facing (OF) conformation for AE1 (SLC4A1) and NBCe1 (SLC4A4) transporters revealed an identical overall fold despite their different transport modes (chloride/bicarbonate exchange versus sodium-carbonate cotransport). However, the exact mechanism determining the different transport modes in the SLC4 family remains unknown. In this work, we report the cryo-EM 3.4 Å structure of the OF conformation of NDCBE (SLC4A8), which shares transport properties with both AE1 and NBCe1 by mediating the electroneutral exchange of sodium-carbonate with chloride. This structure features a fully resolved extracellular loop 3 and well-defined densities corresponding to sodium and carbonate ions in the tentative substrate binding pocket. Further, we combine computational modeling with functional studies to unravel the molecular determinants involved in NDCBE and SLC4 transport.

Suggested Citation

  • Weiguang Wang & Kirill Tsirulnikov & Hristina R. Zhekova & Gülru Kayık & Hanif Muhammad Khan & Rustam Azimov & Natalia Abuladze & Liyo Kao & Debbie Newman & Sergei Yu. Noskov & Z. Hong Zhou & Alexande, 2021. "Cryo-EM structure of the sodium-driven chloride/bicarbonate exchanger NDCBE," Nature Communications, Nature, vol. 12(1), pages 1-12, December.
    • Handle: RePEc:nat:natcom:v:12:y:2021:i:1:d:10.1038_s41467-021-25998-2
    DOI: 10.1038/s41467-021-25998-2
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    Cited by:

    1. Lie Wang & Anthony Hoang & Eva Gil-Iturbe & Arthur Laganowsky & Matthias Quick & Ming Zhou, 2024. "Mechanism of anion exchange and small-molecule inhibition of pendrin," Nature Communications, Nature, vol. 15(1), pages 1-11, December.
    2. Takaaki A. Kobayashi & Hiroto Shimada & Fumiya K. Sano & Yuzuru Itoh & Sawako Enoki & Yasushi Okada & Tsukasa Kusakizako & Osamu Nureki, 2024. "Dimeric transport mechanism of human vitamin C transporter SVCT1," Nature Communications, Nature, vol. 15(1), pages 1-12, December.
    3. Qing Zhang & Liyan Jian & Deqiang Yao & Bing Rao & Ying Xia & Kexin Hu & Shaobai Li & Yafeng Shen & Mi Cao & An Qin & Jie Zhao & Yu Cao, 2023. "The structural basis of the pH-homeostasis mediated by the Cl−/HCO3− exchanger, AE2," Nature Communications, Nature, vol. 14(1), pages 1-11, December.
    4. Yishuo Lu & Peng Zuo & Hongyi Chen & Hui Shan & Weize Wang & Zonglin Dai & He Xu & Yayu Chen & Ling Liang & Dian Ding & Yan Jin & Yuxin Yin, 2023. "Structural insights into the conformational changes of BTR1/SLC4A11 in complex with PIP2," Nature Communications, Nature, vol. 14(1), pages 1-11, December.
    5. Weiqi Zhang & Dian Ding & Yishuo Lu & Hongyi Chen & Peijun Jiang & Peng Zuo & Guangxi Wang & Juan Luo & Yue Yin & Jianyuan Luo & Yuxin Yin, 2024. "Structural and functional insights into the lipid regulation of human anion exchanger 2," Nature Communications, Nature, vol. 15(1), pages 1-10, December.

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