Skip to main content
Log in

The Structural Basis for Coupling of Ca2+ Transport to ATP Hydrolysis by the Sarcoplasmic Reticulum Ca2+-ATPase

  • Published:
Journal of Bioenergetics and Biomembranes Aims and scope Submit manuscript

 

Recently, a series of structure determinations has nearly completed a structural description of the transport cycle of the sarcoplasmic reticulum Ca2+-ATPase, especially those steps concerned with the phosphorylation by ATP and the dephosphorylation reaction. From these structures Ca2+-ATPase emerges as a molecular machine, where globular cytosolic domains and transmembrane helices work in concert like a mechanical pump, as can be vividly demonstrated in animated versions of the pump cycle. The structures show that both ATP phosphorylation and dephosphorylation at Asp351 take place as nucleophilic SN2 reactions, which are associated with Ca2+ and H+ occluded states, respectively. These transitory steps ensure efficient coupling between Ca2+ transport and ATP hydrolysis.

This is a preview of subscription content, log in via an institution to check access.

Access this article

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Similar content being viewed by others

References

  • Andersen, J. P., Lassen, K., and Mòller, J. V. (1985). J. Biol. Chem. 260, 371–380.

    CAS  Google Scholar 

  • Axelsen, K. B., and Palmgren, M. G. (1998). J. Mol. Evol. 46, 84–101.

    Article  CAS  Google Scholar 

  • Clausen, J. D., Vilsen, B., McIntosh, D. B., Einholm, A. P., and Andersen, J. P. (2004). Proc. Natl. Acad. Sci. 101, 2776–2781.

    Article  CAS  Google Scholar 

  • Coan, C., Ji, J.-Y., and Amaral, J. A. (1994). Biochemistry 33, 3722–3731.

    Article  CAS  Google Scholar 

  • Cornelius, F., and Mòller, J. V. (1991). FEBS Lett. 284, 46–50.

    Article  CAS  Google Scholar 

  • Danko, S., Kamidochi, M., Daiho, T., Yamasaki, K., Suzuki, H., and Toyoshima, C. (2001). FEBS Lett. 505, 129–135.

    CAS  Google Scholar 

  • Danko, S., Yamasaki, K., Daiho, T., and Suzuki, H. (2004). J. Biol. Chem. 279, 14991–14998.

    Article  CAS  Google Scholar 

  • Dupont, Y. (1980). Eur. J. Biochem. 109, 231–238.

    Article  CAS  Google Scholar 

  • Forge, V., Mintz, E., and Guillain, F. (1993). J. Biol. Chem. 268, 10953–10968.

    CAS  Google Scholar 

  • Hua, S., Inesi, G., Nomura, H., and Toyoshima, C. (2002). Biochemistry 41, 11405–11410.

    Article  CAS  Google Scholar 

  • Lenoir, G., Picard, M., Gauron, C., Montigny, C., le Marechal, P., Falson, P., le Maire, M., Mòller, J. V., and Champeil, P. (2004). J. Biol. Chem. 279, 9156–9166.

    Article  CAS  Google Scholar 

  • Levy, D., Seigneuret, M., Bluzat, A., and Rigaud, J.-L. (1990). J. Biol. Chem. 265, 19524–19534.

    CAS  Google Scholar 

  • Lutsenko, S., and Kaplan, J. H. (1995). Biochemistry 34, 15607–15613.

    Article  CAS  Google Scholar 

  • Mòller, J. V., Juul, B., and le Maire, M. (1996). Biochim. Biophys. Acta 1286, 1–51.

    Google Scholar 

  • Mòller, J. V., Lenoir, G., Marchand, C., Montigny, C., le Maire, M., Toyoshima, C., Juul, B. S., and Champeil, P. (2002). J. Biol. Chem. 277, 38647–38659.

    Article  Google Scholar 

  • Montigny, C., Jaxel, C., Shainskaya, A., Vinh, J., Labas, V., Mòller, J. V., Karlish, S. J. D., and le Maire, M. (2004). J. Biol. Chem. 279, 43971–43981.

    Article  CAS  Google Scholar 

  • Olesen, C., Sòrensen, T. L.-M., Nielsen, R. C., Mòller, J. V., and Nissen, P. (2004). Science 306, 2251–2255.

    Article  CAS  Google Scholar 

  • Orlowski, S., and Champeil, P. (1991). Biochemistry 30, 352– 361.

    Article  CAS  Google Scholar 

  • Picard, M., Toyoshima, C., and Champeil, P. (2005). J. Biol. Chem. 280, 18745–18754.

    Article  CAS  Google Scholar 

  • Shigekawa, M., and Pearl, M. (1976). J. Biol. Chem. 251, 6947– 6952.

    CAS  Google Scholar 

  • Sòrensen, T. L.-M., Mòller, J. V., and Nissen, P. (2004a). Science 304, 1672–1675.

    Article  CAS  Google Scholar 

  • Sòrensen, T. L.-M., Clausen, J. D., Jensen, A.-M. L., Vilsen, B., Mòller, J. V., Andersen, J. P., and Nissen, P. (2004b). J. Biol. Chem. 279, 46355–46358.

    Article  CAS  Google Scholar 

  • Sugita, Y., Miyashita, N., Ikeguchi, M., Kidera, A., and Toyoshima, C. (2005). J. Am. Chem. Soc. 127, 6150–6151.

    Article  CAS  Google Scholar 

  • Takisawa, H., and Makinose, M. (1983). J. Biol. Chem. 258, 2986– 2992.

    CAS  Google Scholar 

  • Tanford, C. (1983). Annu. Rev. Biochem. 52, 379–409.

    Article  CAS  Google Scholar 

  • Toyoshima, C., and Mizutani, T. (2004). Nature 430, 529–535.

    Article  CAS  Google Scholar 

  • Toyoshima, C., Nakasako, M., Nomura, H., and Ogawa, H. (2000). Nature 405, 647–655.

    Article  CAS  Google Scholar 

  • Toyoshima, C., and Nomura, H. (2002). Nature 418, 605–611.

    Article  CAS  Google Scholar 

  • Toyoshima, C., Nomura, H., and Tsuda, T. (2004). Nature 432, 361–368.

    Article  CAS  Google Scholar 

  • Troullier, A., Girardet, J.-L., and Dupont, Y. (1992). J. Biol. Chem. 267, 22821–22829.

    CAS  Google Scholar 

  • Vilsen, B., and Andersen, J. P. (1992). J. Biol. Chem. 267, 3539–3550.

    CAS  Google Scholar 

  • Wakabayashi, S., and Shigekawa, M. (1990). Biochemistry 29, 7309–7318.

    Article  CAS  Google Scholar 

  • Wang, G., Yamasaki, K., Daiho, T., and Suzuki, H. (2005). J. Biol. Chem. 280, 26508–26576.

    Article  CAS  Google Scholar 

  • White, S. (2005). Membrane proteins of known 3D structure. Available at http://blanco.biomol.uci.edu.

  • Yü, X., Carroll, S., Rigaud, J.-L., and Inesi, G. (1993). Biophys. J. 64, 1232–1242.

    Article  Google Scholar 

  • Yu, X., Hao, L., and Inesi, G. (1994). J. Biol. Chem. 269, 16656–16661.

    CAS  Google Scholar 

Download references

Author information

Authors and Affiliations

Authors

Corresponding author

Correspondence to Jesper Vuust Møller.

Rights and permissions

Reprints and permissions

About this article

Cite this article

Møller, J.V., Olesen, C., Jensen, AM.L. et al. The Structural Basis for Coupling of Ca2+ Transport to ATP Hydrolysis by the Sarcoplasmic Reticulum Ca2+-ATPase. J Bioenerg Biomembr 37, 359–364 (2005). https://doi.org/10.1007/s10863-005-9471-2

Download citation

  • Issue Date:

  • DOI: https://doi.org/10.1007/s10863-005-9471-2

Key Words

Navigation