4HQJ

Crystal structure of Na+,K+-ATPase in the Na+-bound state

Summary for 4HQJ

• Entry DOI: 10.2210/pdb4hqj/pdb
• Descriptor: Sodium/potassium-transporting ATPase subunit alpha-1, Sodium/potassium-transporting ATPase subunit beta-1, Na+/K+ ATPase gamma subunit transcript variant a, ... (8 entities in total)
• Functional Keywords: membrane protein, na+/k+ transport, hydrolase-transport protein complex, hydrolase/transport protein
• Biological source: Sus scrofa (pigs); More
• Cellular location: Cell membrane; Multi-pass membrane protein: P05024; Cell membrane; Single-pass type II membrane protein: P05027
• Total number of polymer chains: 6
• Total formula weight: 313252.18

Authors

Nyblom, M.,Reinhard, L.,Gourdon, P.,Nissen, P. (deposition date: 2012-10-25, release date: 2013-10-02, Last modification date: 2024-11-13)

Primary citation

Nyblom, M.,Poulsen, H.,Gourdon, P.,Reinhard, L.,Andersson, M.,Lindahl, E.,Fedosova, N.,Nissen, P.
Crystal structure of Na+, K(+)-ATPase in the Na(+)-bound state.
Science, 342:123-127, 2013

PubMed 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.

PubMed: 24051246
DOI: 10.1126/science.1243352

Experimental method

X-RAY DIFFRACTION (4.3 Å)