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Poul Nissen

Crystal Structure of Na+, K+-ATPase in the Na+-Bound State

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  • Maria Nyblom, Denmark
  • Hanne Poulsen
  • Pontus Gourdon, Denmark
  • Linda Reinhard (maiden name Schuldt)
  • ,
  • Magnus Andersson, Science for Life Laboratory, Theoretical and Computational Biophysics, Department of Theoretical Physics, Swedish e-Science Research Center, KTH Royal Institute of Technology, Sweden
  • Erik Lindahl, Science for Life Laboratory, Theoretical and Computational Biophysics, Department of Theoretical Physics, Swedish e-Science Research Center, KTH Royal Institute of Technology, Sweden
  • Natalya Fedosova
  • Poul Nissen
The Na(+), K(+)-adenosine triphosphatase (ATPase) maintains the electrochemical gradients of Na(+) and K(+) across the plasma membrane-a prerequisite for electrical excitability and secondary transport. Hitherto, structural information has been limited to K(+)-bound or ouabain-blocked forms. We present the crystal structure of a Na(+)-bound Na(+), K(+)-ATPase as determined at 4.3 Å resolution. Compared with the K(+)-bound form, large conformational changes are observed in the α subunit whereas the β and γ subunit structures are maintained. The locations of the three Na(+) sites are indicated with the unique site III at the recently suggested IIIb, as further supported by electrophysiological studies on leak currents. Extracellular release of the third Na(+) from IIIb through IIIa, followed by exchange of Na(+) for K(+) at sites I and II, is suggested.
Original languageEnglish
JournalScience
Volume342
Issue6154
Pages (from-to)123-127
Number of pages5
ISSN0036-8075
DOIs
Publication statusPublished - 4 Oct 2013

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