ATPases: Ion‐motive

Abstract

Ion motive ATPases allow ion(s) to accumulate on one side of a biological membrane at the expense of ATP hydrolysis. In this way active transport across biological membranes is mediated.

Keywords: active transport; ion; ATP hydrolysis; pump structure; mechanism

Figure 1.

Ca2+ ATPase tertiary structure prediction, redrawn from Green and Stokes . Note the phosphorylation site (D, aspartate) and the nucleotide site (K, lysine)

Figure 2.

Ca2+ ATPase shape, redrawn from Toyoshima et al..

Figure 5.

V‐ATPase motor, redrawn from Boekema et al. . ATP hydrolysis in V1 headpiece induces rotation of the V1 stalk which in turn induces rotation of the V0 rotor. This mechanical energy is used for H+ translocation.

Figure 3.

E1/E2 model for ion transport.

Figure 4.

Function of Na+/K+ ATPase.

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References

Boekema EJ, Ubbink‐Kok T, Lolkema JS, Brisson A and Konings WN (1997) Visualisation of a peripheral stalk in V‐type ATPase: evidence for the stator structure essential to rotational catalysis. Proceedings of the National Academy of Sciences of the USA 94: 14291–14293.

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Green NM and Stokes DL (1992) Structural modelling of P‐type ion pumps. Acta Physiologica Scandinavia 146: 59–68.

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Further Reading

Bittar EE and Andersen JP (eds) (1998) Ion pumps. A special volume of Advances in Molecular and Cell Biology, vols 23A and 23B. London: JAI Press.

Skou JC and Esmann M (1992) The Na+, K+‐ATPase. Journal of Bioenergetics and Biomembranes 24: 249–261.

Solioz M and Vulpe C (1996) CPx‐type ATPases: a class of P‐type ATPases that pump heavy metals. Trends in Biochemical Sciences 21: 237–241.

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How to Cite close
Guillain, Florent, and Mintz, Elisabeth(Apr 2001) ATPases: Ion‐motive. In: eLS. John Wiley & Sons Ltd, Chichester. http://www.els.net [doi: 10.1038/npg.els.0000678]