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7.2.2.13: Na+/K+-exchanging ATPase

This is an abbreviated version!
For detailed information about Na+/K+-exchanging ATPase, go to the full flat file.

Word Map on EC 7.2.2.13

Reaction

ATP
+
H2O
 +
Na+[side 1]
 +
K+[side 2]
=
ADP
 +
phosphate
 +
Na+[side 2]
 +
K+[side 1]

Synonyms

(Na+ + K+)-activated ATPase, (Na+ + K+)-ATPase, (Na+, K+)-ATPase, (Na+, K+)-dependent ATPase, (Na+,K+)-activated ATPase, (Na+-K+)-ATPase, alpha2Na+/K+-ATPase, ATP1a1, atp1a1a, ATPalpha, EC 3.6.1.3, EC 3.6.1.37, EC 3.6.3.9, Na pump, Na(+)-K(+)-exchanging ATPase, Na+ pump, Na+, K+ -ATPase, Na+, K+-ATPase, Na+,K+ pump, Na+,K+-adenosine triphosphatase, Na+,K+-ATPase, Na+,K+-pump, Na+-K+ ATPase, Na+-K+ pump, Na+-K+ pump alpha1-isoform, Na+-K+ pump alpha2-isoform, Na+-K+-ATPase, Na+-K+-ATPase alpha2-isoform, Na+-K+-pump, Na+/K+ -ATPase, Na+/K+ ATPase, Na+/K+ pump, Na+/K+-ATPase, Na+K+-ATPase, Na+K+ATPase, Na, K-ATPase, Na,K pump, Na,K-activated ATPase, Na,K-adenosine triphosphatase, Na,K-ATPase, Na,K-Pump, Na-K-ATPase, Na/K pump, Na/K-ATPase, NKA, Nkaalpha protein, nkaalpha1, nkaalpha3a, nkaalpha3b, renal sodium-potassium pump, SNaK1, sodium potassium adenosinetriphosphatase, sodium pump, sodium-potassium pump, sodium/potassium ATPase

ECTree

     7 Translocases
         7.2 Catalysing the translocation of inorganic cations
             7.2.2 Linked to the hydrolysis of a nucleoside triphosphate
                7.2.2.13 Na+/K+-exchanging ATPase

Crystallization

Crystallization on EC 7.2.2.13 - Na+/K+-exchanging ATPase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
in complex with beryllium fluoride, ouabain, and Mg2+, hanging drop vapor diffusion method, using 14% (w/v) PEG 3350, 100 mM MOPS/N-methyl-d-glucamine pH 7.0, 210 mM MgCl2, 25mM 2-mercaptoethanol
Q08DA1; G3MWR4; Q04645
strucutural modeling of enzyme. Residue F785 participates in a hydrophobic network between three transmembrane segments. Residue T618 is located in the cytoplasmic part of the molecule near the catalyitc site
-
two-stage model of interaction between cardiac transmembrane protein phospholemman and the Na+/K+-ATPase involving phospholemman-ATPase interaction and subsequent formation of an unstable phospholemman trimer, which readily interacts with surrounding ATPase molecules
-
refinement to 9-11 A
-
Na+,K+-ATPase with bound inhibitor ouabain fixed in a state analogous to E2-2K+Pi with a stable phosphate analog MgF4 2-, usage of the crystallization buffer containing 25% glycerol w/v, 5% v/v MPD, 100 mM potassium acetate, 10 mM KCl, 4 mM MgCl2, 4 mM KF, 0.1 mM EGTA, 10 mM glutathione, 0.002 mg/mL 2,6-di-t-butyl-p-cresol, 20 mM MES-Tris, pH 7.0, and 40% w/v PEG 3000, soaking of the crystals in a buffer containing 20 mM ouabain for 5 h, X-ray diffraction structure determination and analysis at 2.8 A resolution
4.6 A resolution crystal structure in its phosphorylated form stabilized by high affinity binding of ouabain. Ouabain binds to a site formed at transmembrane segments alphaM1-alphaM6, plugging the ion pathway from the extracellular side. The A domain has rotated in response to phosphorylation and alphaM1-2 move towards the ouabain molecule, providing for high affinity interactions and closing the ion pathway from the extracellular side
E2P enzyme form in complex with inhibitors, hanging drop vapor diffusion method, using 17% (w/v) PEG 2000 monomethyl ether, 10% (v/v) glycerol, 220 mM MgCl2,100 mM KCl, 100 mM MES (titrated with KOH, pH 6.2), 5% (v/v) 2-methyl-2,4-pentanediol, and 6% (v/v) Jeffamine M-600 (titrated with KOH, pH 6.2)
enzyme with bound Na+, ADP and aluminium fluoride, a stable phosphate analogue, with and without oligomycin, vapor diffusion method
-
purified native enzyme, X-ray diffraction structure determination and analysis at 2.0-3.0 A resolution, molecular replacement, the NKA monomer is divided into four separate domain masks
-