IDEAS home Printed from https://ideas.repec.org/a/nat/natcom/v13y2022i1d10.1038_s41467-022-32990-x.html
   My bibliography  Save this article

Structural basis for gating mechanism of the human sodium-potassium pump

Author

Listed:
  • Phong T. Nguyen

    (University of Texas Southwestern Medical Center)

  • Christine Deisl

    (University of Texas Southwestern Medical Center)

  • Michael Fine

    (University of Texas Southwestern Medical Center)

  • Trevor S. Tippetts

    (University of Texas Southwestern Medical Center)

  • Emiko Uchikawa

    (University of Texas Southwestern Medical Center)

  • Xiao-chen Bai

    (University of Texas Southwestern Medical Center)

  • Beth Levine

    (University of Texas Southwestern Medical Center)

Abstract

P2-type ATPase sodium-potassium pumps (Na+/K+-ATPases) are ion-transporting enzymes that use ATP to transport Na+ and K+ on opposite sides of the lipid bilayer against their electrochemical gradients to maintain ion concentration gradients across the membranes in all animal cells. Despite the available molecular architecture of the Na+/K+-ATPases, a complete molecular mechanism by which the Na+ and K+ ions access into and are released from the pump remains unknown. Here we report five cryo-electron microscopy (cryo-EM) structures of the human alpha3 Na+/K+-ATPase in its cytoplasmic side-open (E1), ATP-bound cytoplasmic side-open (E1•ATP), ADP-AlF4− trapped Na+-occluded (E1•P-ADP), BeF3− trapped exoplasmic side-open (E2P) and MgF42− trapped K+-occluded (E2•Pi) states. Our work reveals the atomically resolved structural detail of the cytoplasmic gating mechanism of the Na+/K+-ATPase.

Suggested Citation

  • Phong T. Nguyen & Christine Deisl & Michael Fine & Trevor S. Tippetts & Emiko Uchikawa & Xiao-chen Bai & Beth Levine, 2022. "Structural basis for gating mechanism of the human sodium-potassium pump," Nature Communications, Nature, vol. 13(1), pages 1-12, December.
    • Handle: RePEc:nat:natcom:v:13:y:2022:i:1:d:10.1038_s41467-022-32990-x
    DOI: 10.1038/s41467-022-32990-x
    as

    Download full text from publisher

    File URL: https://www.nature.com/articles/s41467-022-32990-x
    File Function: Abstract
    Download Restriction: no
    File URL: https://libkey.io/10.1038/s41467-022-32990-x?utm_source=ideas
    LibKey link: if access is restricted and if your library uses this service, LibKey will redirect you to where you can use your library subscription to access this item
    ---><---

    References listed on IDEAS

    as
    1. Takehiro Shinoda & Haruo Ogawa & Flemming Cornelius & Chikashi Toyoshima, 2009. "Crystal structure of the sodium–potassium pump at 2.4 Å resolution," Nature, Nature, vol. 459(7245), pages 446-450, May.
    2. J. Preben Morth & Bjørn P. Pedersen & Mads S. Toustrup-Jensen & Thomas L.-M. Sørensen & Janne Petersen & Jens Peter Andersen & Bente Vilsen & Poul Nissen, 2007. "Crystal structure of the sodium–potassium pump," Nature, Nature, vol. 450(7172), pages 1043-1049, December.
    3. Ryuta Kanai & Haruo Ogawa & Bente Vilsen & Flemming Cornelius & Chikashi Toyoshima, 2013. "Crystal structure of a Na+-bound Na+,K+-ATPase preceding the E1P state," Nature, Nature, vol. 502(7470), pages 201-206, October.
    4. Claus Olesen & Martin Picard & Anne-Marie Lund Winther & Claus Gyrup & J. Preben Morth & Claus Oxvig & Jesper Vuust Møller & Poul Nissen, 2007. "The structural basis of calcium transport by the calcium pump," Nature, Nature, vol. 450(7172), pages 1036-1042, December.
    5. Mateusz Dyla & Daniel S. Terry & Magnus Kjaergaard & Thomas L.-M. Sørensen & Jacob Lauwring Andersen & Jens P. Andersen & Charlotte Rohde Knudsen & Roger B. Altman & Poul Nissen & Scott C. Blanchard, 2017. "Dynamics of P-type ATPase transport revealed by single-molecule FRET," Nature, Nature, vol. 551(7680), pages 346-351, November.
    6. Kazuhiro Abe & Katsumasa Irie & Hanayo Nakanishi & Hiroshi Suzuki & Yoshinori Fujiyoshi, 2018. "Crystal structures of the gastric proton pump," Nature, Nature, vol. 556(7700), pages 214-218, April.
    Full references (including those not matched with items on IDEAS)

    Most related items

    These are the items that most often cite the same works as this one and are cited by the same works as this one.
    1. Yingying Guo & Yuanyuan Zhang & Renhong Yan & Bangdong Huang & Fangfei Ye & Liushu Wu & Ximin Chi & Yi shi & Qiang Zhou, 2022. "Cryo-EM structures of recombinant human sodium-potassium pump determined in three different states," Nature Communications, Nature, vol. 13(1), pages 1-9, December.
    2. Victoria C. Young & Hanayo Nakanishi & Dylan J. Meyer & Tomohiro Nishizawa & Atsunori Oshima & Pablo Artigas & Kazuhiro Abe, 2022. "Structure and function of H+/K+ pump mutants reveal Na+/K+ pump mechanisms," Nature Communications, Nature, vol. 13(1), pages 1-15, December.
    3. Zongxin Guo & Fredrik Orädd & Viktoria Bågenholm & Christina Grønberg & Jian Feng Ma & Peter Ott & Yong Wang & Magnus Andersson & Per Amstrup Pedersen & Kaituo Wang & Pontus Gourdon, 2024. "Diverse roles of the metal binding domains and transport mechanism of copper transporting P-type ATPases," Nature Communications, Nature, vol. 15(1), pages 1-16, December.
    4. Bjørn P Pedersen & Georgiana Ifrim & Poul Liboriussen & Kristian B Axelsen & Michael G Palmgren & Poul Nissen & Carsten Wiuf & Christian N S Pedersen, 2014. "Large Scale Identification and Categorization of Protein Sequences Using Structured Logistic Regression," PLOS ONE, Public Library of Science, vol. 9(1), pages 1-11, January.
    5. Peng Zhao & Chaoran Zhao & Dandan Chen & Caihong Yun & Huilin Li & Lin Bai, 2021. "Structure and activation mechanism of the hexameric plasma membrane H+-ATPase," Nature Communications, Nature, vol. 12(1), pages 1-11, December.
    6. Takuto Fujii & Shushi Nagamori & Pattama Wiriyasermkul & Shizhou Zheng & Asaka Yago & Takahiro Shimizu & Yoshiaki Tabuchi & Tomoyuki Okumura & Tsutomu Fujii & Hiroshi Takeshima & Hideki Sakai, 2023. "Parkinson’s disease-associated ATP13A2/PARK9 functions as a lysosomal H+,K+-ATPase," Nature Communications, Nature, vol. 14(1), pages 1-11, December.
    7. Jianqiang Mu & Chenyang Xue & Lei Fu & Zongjun Yu & Minhan Nie & Mengqi Wu & Xinmeng Chen & Kun Liu & Ruiqian Bu & Ying Huang & Baisheng Yang & Jianming Han & Qianru Jiang & Kevin C. Chan & Ruhong Zho, 2023. "Conformational cycle of human polyamine transporter ATP13A2," Nature Communications, Nature, vol. 14(1), pages 1-12, December.

    More about this item

    Statistics

    Access and download statistics

    Corrections

    All material on this site has been provided by the respective publishers and authors. You can help correct errors and omissions. When requesting a correction, please mention this item's handle: RePEc:nat:natcom:v:13:y:2022:i:1:d:10.1038_s41467-022-32990-x. See general information about how to correct material in RePEc.

    If you have authored this item and are not yet registered with RePEc, we encourage you to do it here. This allows to link your profile to this item. It also allows you to accept potential citations to this item that we are uncertain about.

    If CitEc recognized a bibliographic reference but did not link an item in RePEc to it, you can help with this form .

    If you know of missing items citing this one, you can help us creating those links by adding the relevant references in the same way as above, for each refering item. If you are a registered author of this item, you may also want to check the "citations" tab in your RePEc Author Service profile, as there may be some citations waiting for confirmation.

    For technical questions regarding this item, or to correct its authors, title, abstract, bibliographic or download information, contact: Sonal Shukla or Springer Nature Abstracting and Indexing (email available below). General contact details of provider: http://www.nature.com .

    Please note that corrections may take a couple of weeks to filter through the various RePEc services.

    IDEAS is a RePEc service. RePEc uses bibliographic data supplied by the respective publishers.