3B8E

Crystal structure of the sodium-potassium pump

3B8E の概要

• エントリーDOI: 10.2210/pdb3b8e/pdb
• 分子名称: 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)
• 機能のキーワード: na+, k+-atpase, p-type atpase, cation pump, membrane protein, hydrolase, atp-binding, calcium transport, ion transport, membrane potential, phosphorylation, magnesium, metal-binding, nucleotide-binding, potassium, potassium transport, sodium, sodium transport, sodium/potassium transport, transmembrane, glycoprotein, signal-anchor, hydrolase-transport protein complex, hydrolase/transport protein
• 由来する生物種: Sus scrofa (pig); 詳細
• 細胞内の位置: Cell membrane; Multi-pass membrane protein: P05024; Membrane; Single-pass type II membrane protein: P05027
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 239878.01

構造登録者

Morth, J.P.,Pedersen, P.B.,Toustrup-Jensen, M.S.,Soerensen, T.L.M.,Petersen, J.,Andersen, J.P.,Vilsen, B.,Nissen, P. (登録日: 2007-11-01, 公開日: 2007-12-18, 最終更新日: 2024-03-13)

主引用文献

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

実験手法

X-RAY DIFFRACTION (3.5 Å)