Ion Motive ATPases: P‐type ATPases

Abstract

Regulation of ions such as calcium, sodium and potassium ions is very important for cell life. One of ion‐regulating enzymes is classified as ion motive adenosine triphosphatase (ATPase). Ion motive ATPases exchange two different ions across the membrane at the expense of ATP energy. The Ca2+‐ATPase transports Ca ion in exchange for H ion; the Na+/K+ or H+/K+ATPase transports Na ion or hydronium ion from the cytoplasmic region to the exocytoplasmic region with the exchange of K ion from the exoplasmic domain to the cytoplasmic domain. The Ca2+‐ATPase has single catalytic subunit. The Na+/K+ and H+/K+ATPases consist of two subunits α and β. The α subunit is the catalytic subunit, having 10 transmembrane domains. The β subunit is a glycosylated protein.

Key concepts

  • Ion motive ATPases

  • P‐type ATPase transport ions across the membrane

  • Regulating ion concentrations.

Keywords: pumps; ATPase; P‐type

Figure 1.

The various types of eukaryotic P2‐ATPases. The electrogenic yeast H+‐ATPase, the Ca2+‐ATPase, the Na+/K+‐ATPase and gastric H+/K+‐ATPase are illustrated. Among these ATPases, only the gastric H+/K+‐ATPase is electroneutral.

Figure 2.

The reaction steps of a typical countertransport P2‐ATPase such as the gastric H+/K+‐ATPase. The reaction starts (top centre) by binding of the primary transport cation. This is followed by phosphorylation, occlusion (centre of figure) and change of sidedness of the binding site. After release of the initial cation, the countertransport cation is bound, the enzyme dephosphorylates and the counter‐ion moves to the other side of the enzyme.

Figure 3.

SERCA1a structures representing key states of the reaction cycle. Cation‐ and nucleotide‐exchange reactions are indicated. The structures are depicted by grey, transparent surfaces and by cartoon representations, with the A‐domain in yellow, N‐domain in red, P‐domain in blue, transmembrane segment M1–M2 in purple, M3–M4 in green, M5–M6 in wheat and M7–M10 in grey. Each model of the structure is based on the work of Olesen et al..

Figure 4.

Structure of the Na+/K+‐ATPase αβγ complex. Cytoplasmic domain consists of N‐, A‐ and P‐domains. In the membrane domain, there are 10 transmembrane segments in the α subunit, 1 transmembrane segment each in the β and γ subunit. Carbohydrates are attached to the β subunit in the extracellular domain. This structure model is based on the work of Morth et al..

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Further Reading

Hou Z and Mitra B (2003) The metal specificity and selectivity of ZntA from E. coli using the acylphosphate intermediate. Journal of Biological Chemistry 278: 28455–28461.

Zhang Z, Zheng Y, Mazon H et al. (2008) Structure of the yeast vacuolar ATPase. Journal of Biological Chemistry 283: 35983–35995.

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Shin, Jai Moo, and Sachs, George(Sep 2009) Ion Motive ATPases: P‐type ATPases. In: eLS. John Wiley & Sons Ltd, Chichester. http://www.els.net [doi: 10.1002/9780470015902.a0001379.pub2]