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

Maria Nyblom; Hanne Poulsen; Pontus Gourdon; Linda Reinhard (maiden name Schuldt); Magnus Andersson; Erik Lindahl; Natalya Fedosova; Poul Nissen

doi:10.1126/science.1243352

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

Maria Nyblom, Hanne Poulsen, Pontus Gourdon, Linda Reinhard (maiden name Schuldt), Magnus Andersson, Erik Lindahl, Natalya Fedosova, Poul Nissen

Research output: Contribution to journal/Conference contribution in journal/Contribution to newspaper › Journal article › Research › peer-review

Abstract

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 language	English
Journal	Science
Volume	342
Issue	6154
Pages (from-to)	123-127
Number of pages	5
ISSN	0036-8075
DOIs	https://doi.org/10.1126/science.1243352
Publication status	Published - 4 Oct 2013

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

abstract = "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 {\AA} 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.",

author = "Maria Nyblom and Hanne Poulsen and Pontus Gourdon and {Reinhard (maiden name Schuldt)}, Linda and Magnus Andersson and Erik Lindahl and Natalya Fedosova and Poul Nissen",

year = "2013",

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doi = "10.1126/science.1243352",

language = "English",

volume = "342",

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TY - JOUR

T1 - Crystal Structure of Na+, K+-ATPase in the Na+-Bound State

AU - Nyblom, Maria

AU - Poulsen, Hanne

AU - Gourdon, Pontus

AU - Reinhard (maiden name Schuldt), Linda

AU - Andersson, Magnus

AU - Lindahl, Erik

AU - Fedosova, Natalya

AU - Nissen, Poul

PY - 2013/10/4

Y1 - 2013/10/4

N2 - 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.

AB - 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.

U2 - 10.1126/science.1243352

DO - 10.1126/science.1243352

M3 - Journal article

C2 - 24051246

SN - 0036-8075

VL - 342

SP - 123

EP - 127

JO - Science

JF - Science

IS - 6154

ER -

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

Abstract

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