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Crystal Structure of Na+, K+-ATPase in the Na+-Bound State
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2013 (English)In: Science, ISSN 0036-8075, E-ISSN 1095-9203, Vol. 342, no 6154, 123-127 p.Article in journal (Refereed) Published
Abstract [en]

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 angstrom resolution. Compared with the K+-bound form, large conformational changes are observed in the a subunit whereas the beta and gamma 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.

Place, publisher, year, edition, pages
2013. Vol. 342, no 6154, 123-127 p.
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Biological Sciences
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URN: urn:nbn:se:su:diva-95747DOI: 10.1126/science.1243352ISI: 000325126100060OAI: oai:DiVA.org:su-95747DiVA: diva2:662282
Note

AuthorCount:8;

Available from: 2013-11-06 Created: 2013-11-04 Last updated: 2017-12-06Bibliographically approved

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Lindahl, Erik
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Department of Biochemistry and BiophysicsScience for Life Laboratory (SciLifeLab)
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