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Crystal structure of the potassium-importing KdpFABC membrane complex

Author

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  • Ching-Shin Huang

    (Molecular Biophysics Graduate Program, New York University School of Medicine, Skirball Institute)

  • Bjørn Panyella Pedersen

    (Aarhus University
    Aarhus Institute of Advanced Studies, Aarhus University)

  • David L. Stokes

    (New York University School of Medicine, Skirball Institute)

Abstract

The crystal structure of the bacterial potassium import complex KdpFABC shows how ATP hydrolysis is coupled to potassium transport to maintain cellular homeostasis under low potassium conditions.

Suggested Citation

  • Ching-Shin Huang & Bjørn Panyella Pedersen & David L. Stokes, 2017. "Crystal structure of the potassium-importing KdpFABC membrane complex," Nature, Nature, vol. 546(7660), pages 681-685, June.
    • Handle: RePEc:nat:nature:v:546:y:2017:i:7660:d:10.1038_nature22970
    DOI: 10.1038/nature22970
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    Cited by:

    1. Jakob M. Silberberg & Sophie Ketter & Paul J. N. Böhm & Kristin Jordan & Marcel Wittenberg & Julia Grass & Inga Hänelt, 2024. "KdpD is a tandem serine histidine kinase that controls K+ pump KdpFABC transcriptionally and post-translationally," Nature Communications, Nature, vol. 15(1), pages 1-12, December.

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