3KDP

Crystal structure of the sodium-potassium pump

Summary for 3KDP

• Entry DOI: 10.2210/pdb3kdp/pdb
• Related: 3B8E 3FGO
• Descriptor: Sodium/potassium-transporting ATPase subunit alpha-1, Sodium/potassium-transporting ATPase subunit beta-1, Na+/K+ ATPase gamma subunit transcript variant a, ... (7 entities in total)
• Functional Keywords: alpha helical, heterotrimeric membrane protein complex, atp-binding, hydrolase, ion transport, magnesium, membrane, metal-binding, nucleotide-binding, phosphoprotein, potassium, potassium transport, sodium transport, sodium/potassium transport, transmembrane, transport, disulfide bond, glycoprotein, signal-anchor
• Biological source: Sus scrofa (Pig); More
• Cellular location: Cell membrane, sarcolemma ; Multi-pass membrane protein : P05024; Cell membrane ; Single-pass type II membrane protein : P05027
• Total number of polymer chains: 6
• Total formula weight: 294289.74

Authors

Morth, J.P.,Pedersen, B.P.,Nissen, P. (deposition date: 2009-10-23, release date: 2010-02-16, Last modification date: 2024-10-30)

Primary citation

Morth, J.P.,Pedersen, B.P.,Toustrup-Jensen, M.S.,Sorensen, T.L.,Petersen, J.,Andersen, J.P.,Vilsen, B.,Nissen, P.
Crystal structure of the sodium-potassium pump.
Nature, 450:1043-1049, 2007

PubMed Abstract: The Na+,K+-ATPase generates electrochemical gradients for sodium and potassium that are vital to animal cells, exchanging three sodium ions for two potassium ions across the plasma membrane during each cycle of ATP hydrolysis. Here we present the X-ray crystal structure at 3.5 A resolution of the pig renal Na+,K+-ATPase with two rubidium ions bound (as potassium congeners) in an occluded state in the transmembrane part of the alpha-subunit. Several of the residues forming the cavity for rubidium/potassium occlusion in the Na+,K+-ATPase are homologous to those binding calcium in the Ca2+-ATPase of sarco(endo)plasmic reticulum. The beta- and gamma-subunits specific to the Na+,K+-ATPase are associated with transmembrane helices alphaM7/alphaM10 and alphaM9, respectively. The gamma-subunit corresponds to a fragment of the V-type ATPase c subunit. The carboxy terminus of the alpha-subunit is contained within a pocket between transmembrane helices and seems to be a novel regulatory element controlling sodium affinity, possibly influenced by the membrane potential.

PubMed: 18075585
DOI: 10.1038/nature06419

Experimental method

X-RAY DIFFRACTION (3.5 Å)