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Crystal structure of the plasma membrane proton pump

Author

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  • Bjørn P. Pedersen

    (Centre for Membrane Pumps in Cells and Disease—PUMPKIN. Danish National Research Foundation,
    University of Aarhus, Gustav Wieds Vej 10C, DK-8000 Aarhus, Denmark)

  • Morten J. Buch-Pedersen

    (Centre for Membrane Pumps in Cells and Disease—PUMPKIN. Danish National Research Foundation,
    University of Aarhus, Gustav Wieds Vej 10C, DK-8000 Aarhus, Denmark
    Plant Physiology and Anatomy Laboratory, University of Copenhagen, Thorvaldsensvej 40, DK-1871 Frederiksberg, Denmark)

  • J. Preben Morth

    (Centre for Membrane Pumps in Cells and Disease—PUMPKIN. Danish National Research Foundation,
    University of Aarhus, Gustav Wieds Vej 10C, DK-8000 Aarhus, Denmark)

  • Michael G. Palmgren

    (Centre for Membrane Pumps in Cells and Disease—PUMPKIN. Danish National Research Foundation,
    Plant Physiology and Anatomy Laboratory, University of Copenhagen, Thorvaldsensvej 40, DK-1871 Frederiksberg, Denmark)

  • Poul Nissen

    (Centre for Membrane Pumps in Cells and Disease—PUMPKIN. Danish National Research Foundation,
    University of Aarhus, Gustav Wieds Vej 10C, DK-8000 Aarhus, Denmark)

Abstract

Pumping Ions P-type ATPases are cation pumps of fundamental importance for all eukaryotes and many prokaryotes. Three papers this week present structural and functional studies of key members of this superfamily. The cover shows the Na+,K+-pump structure, described at 3.5 Å resolution by Morth et al., together with J. C. Skou's original notes on his discovery of its Na+- and K+-dependent ATPase activity 50 years ago. The paper reveals the potassium-bound state and hints at a voltage-dependent basis of regulation, in part through kinetic experiments similar to Skou's. Olesen et al. have obtained crystallographic snapshots of the sarcoplasmic reticulum Ca2+-ATPase, the calcium pump, complemented by functional studies, and a complete mechanism of calcium transport is finally presented. In plants and fungi, cellular ion homeostasis and membrane potential are powered by the plasma membrane H+-ATPase — another P-type ATPase. Pedersen et al. present its X-ray structure and provide insight into how it pumps protons against a steep electrochemical gradient.

Suggested Citation

  • Bjørn P. Pedersen & Morten J. Buch-Pedersen & J. Preben Morth & Michael G. Palmgren & Poul Nissen, 2007. "Crystal structure of the plasma membrane proton pump," Nature, Nature, vol. 450(7172), pages 1111-1114, December.
    • Handle: RePEc:nat:nature:v:450:y:2007:i:7172:d:10.1038_nature06417
    DOI: 10.1038/nature06417
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    Citations

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    Cited by:

    1. 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.
    2. Hong Il Choi & Sung-Won Hwang & Jongrae Kim & Byeonghyeok Park & EonSeon Jin & In-Geol Choi & Sang Jun Sim, 2021. "Augmented CO2 tolerance by expressing a single H+-pump enables microalgal valorization of industrial flue gas," Nature Communications, Nature, vol. 12(1), pages 1-15, December.
    3. 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.
    4. Saashia Fuji & Shota Yamauchi & Naoyuki Sugiyama & Takayuki Kohchi & Ryuichi Nishihama & Ken-ichiro Shimazaki & Atsushi Takemiya, 2024. "Light-induced stomatal opening requires phosphorylation of the C-terminal autoinhibitory domain of plasma membrane H+-ATPase," Nature Communications, Nature, vol. 15(1), pages 1-13, December.
    5. 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.

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