Mechanism of the Na+, K+ pump. Protein structure and conformations of the pure (Na+ +K+)-ATPase.

@article{Jrgensen1982MechanismOT,
  title={Mechanism of the Na+, K+ pump. Protein structure and conformations of the pure (Na+ +K+)-ATPase.},
  author={P. L. J{\o}rgensen},
  journal={Biochimica et biophysica acta},
  year={1982},
  volume={694 1},
  pages={
          27-68
        }
}

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References

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Crystallization patterns of membrane-bound (Na+ +K+)-ATPase.
TLDR
Computer-averaged images of the two-dimensional crystals show that the unit cell in vanadate-induced crystals contains a protomericalpha beta-unit of the enzyme protein, suggesting the interactions between alpha beta-units can be of importance in the function of the Na+, K+ pump. Expand
Mechanisms for the incorporation of proteins in membranes and organelles
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Mechanisms for the transfer of newly synthesized polypeptides to their sites of function in different subcellular membranes and organelles are considered, and models in which specific features of the polypePTides serve as signals to direct them along selected sub cellular pathways to their final destination are discussed. Expand
(Na+ + K+) ATPase has one functioning phosphorylation site per α subunit
(Na+ + K+)ATPase contains two different subunits, a catalytic subunit (α) and a subunit with uncertain function (β). The enzyme binds ATP, ouabain and vanadate, and can be phos-phorylated by ATP asExpand
(Na+ + K+)-ATPase : phosphorylation-dependent cross-linking of the alpha-subunits in the presence of Ca2+ and o-phenanthroline.
TLDR
Results indicate that it is the formation of phosphoenzyme per se that leads to conformational transitions favorable to cross-linking, and suggest that Cu2+ and o-phenanthroline participate in the cross- linking reaction, but not in the phosphorylation reactions. Expand
Characterization of 2',3'-O-(2,4,6-trinitrocyclohexadienylidine)adenosine 5'-triphosphate as a fluorescent probe of the ATP site of sodium and potassium transport adenosine triphosphatase. Determination of nucleotide binding stoichiometry and ion-induced changes in affinity for ATP.
TLDR
The results suggests that a single ATP site exhibits a high or low affinity for ATP depending on the ligands present, so that high and low affinity ATP sites observed kinetically are interconvertible and do not co-exist independently. Expand
Conformational changes of renal sodium plus potassium ion-transport adenosine triphosphatase labeled with fluorescein.
TLDR
Five conformational changes of purified renal sodium plus potassium ion-transport adenosine triphosphatase (ATP phosphohydrolase, EC 3.6.1.3) labeled with fluorescein isothiocyanate are studied, finding that low and high affinity for Mg2+ alternates as the enzyme turns over, Mg 2+ may be bound and released sequentially during the catalytic cycle. Expand
Eosin, a fluorescent probe of ATP binding to the (Na+ + K+)-ATPase.
TLDR
The results suggest that the high affinity eosin binding site is an ATP binding site and that it is located on the enzyme in an environment with a low polarity. Expand
Formation of two‐dimensional crystals in pure membrane‐bound Na+,K+‐ATPase
TLDR
Negative staining is used to monitor the aggregation of the protein units during exposure to different combinations of the specific ligands of Na+,K÷-ATPase and it is suggested that transition to the vanadate-bound Erform of the enzyme protein favours immobilization of the units in crystalline arrays. Expand
Inhibition of sodium and potassium adenosine triphosphatase by 2',3'-O-(2,4,6-trinitrocyclohexadienylidene) adenine nucleotides. Implications for the structure and mechanism of the Na:K pump.
TLDR
It is concluded that high and low affinity ATP "sites" are interconvertible (i.e. they represent two forms of the same site) and do not co-exist independently. Expand
K+-independent active transport of Na+ by the (Na+ and K+)-stimulated adenosine triphosphatase.
The (Na+ and K+)-stimulated adenosine triphosphatase (Na+,K+)-ATPase) from canine kidney reconstituted into phospholipid vesicles showed an ATP-dependent, ouabain-inhibited uptake of 22Na+ in theExpand
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