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The sarcoplasmic Ca2+-ATPase: design of a perfect chemi-osmotic pump

Published online by Cambridge University Press:  01 September 2010

Jesper V. Møller ,
Claus Olesen ,
Anne-Marie L. Winther  and
Poul Nissen
Jesper V. Møller*
Affiliation:
Centre for Membrane Pumps in Cells and Disease – PUMPKIN, Danish National Research Foundation, Denmark Department of Physiology and Biophysics, Aarhus University, Ole Worms Alle 6, 1180, DK-8000 Aarhus C, Denmark
Claus Olesen*
Affiliation:
Centre for Membrane Pumps in Cells and Disease – PUMPKIN, Danish National Research Foundation, Denmark Department of Physiology and Biophysics, Aarhus University, Ole Worms Alle 6, 1180, DK-8000 Aarhus C, Denmark
Anne-Marie L. Winther
Affiliation:
Centre for Membrane Pumps in Cells and Disease – PUMPKIN, Danish National Research Foundation, Denmark Department of Molecular Biology, Aarhus University, Gustav Wieds Vej 10C, DK-8000 Aarhus C, Denmark
Poul Nissen
Affiliation:
Centre for Membrane Pumps in Cells and Disease – PUMPKIN, Danish National Research Foundation, Denmark Department of Molecular Biology, Aarhus University, Gustav Wieds Vej 10C, DK-8000 Aarhus C, Denmark
*
*Authors for correspondence: Jesper V. Møller and Claus Olesen. Email: [email protected] and [email protected]
*Authors for correspondence: Jesper V. Møller and Claus Olesen. Email: [email protected] and [email protected]
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Abstract

The sarcoplasmic (SERCA 1a) Ca2+-ATPase is a membrane protein abundantly present in skeletal mucles where it functions as an indispensable component of the excitation–contraction coupling, being at the expense of ATP hydrolysis involved in Ca2+/H+ exchange with a high thermodynamic efficiency across the sarcoplasmic reticulum membrane. The transporter serves as a prototype of a whole family of cation transporters, the P-type ATPases, which in addition to Ca2+ transporting proteins count Na+, K+-ATPase and H+, K+-, proton- and heavy metal transporting ATPases as prominent members. The ability in recent years to produce and analyze at atomic (2·3–3 Å) resolution 3D-crystals of Ca2+-transport intermediates of SERCA 1a has meant a breakthrough in our understanding of the structural aspects of the transport mechanism. We describe here the detailed construction of the ATPase in terms of one membraneous and three cytosolic domains held together by a central core that mediates coupling between Ca2+-transport and ATP hydrolysis. During turnover, the pump is present in two different conformational states, E1 and E2, with a preference for the binding of Ca2+ and H+, respectively. We discuss how phosphorylated and non-phosphorylated forms of these conformational states with cytosolic, occluded or luminally exposed cation-binding sites are able to convert the chemical energy derived from ATP hydrolysis into an electrochemical gradient of Ca2+ across the sarcoplasmic reticulum membrane. In conjunction with these basic reactions which serve as a structural framework for the transport function of other P-type ATPases as well, we also review the role of the lipid phase and the regulatory and thermodynamic aspects of the transport mechanism.

Type
Review Article
Information
Quarterly Reviews of Biophysics , Volume 43 , Issue 4 , November 2010 , pp. 501 - 566
Copyright
Copyright © Cambridge University Press 2010

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