Dynamics of P-type ATPase transport revealed by single-molecule FRET

Mateusz Dyla, Daniel S. Terry, Magnus Kjaergaard, Thomas L.-M. Sørensen, Jacob Lauwring Andersen, Jens P. Andersen, Charlotte Rohde Knudsen, Roger B. Altman, Poul Nissen () and Scott C. Blanchard ()
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Mateusz Dyla: Centre for Membrane Pumps in Cells and Disease – PUMPKIN, Danish National Research Foundation & Danish Research Institute of Translational Neuroscience – DANDRITE, Nordic-EMBL Partnership for Molecular Medicine, Aarhus University
Daniel S. Terry: Weill Cornell Medicine, Cornell University
Magnus Kjaergaard: Centre for Membrane Pumps in Cells and Disease – PUMPKIN, Danish National Research Foundation & Danish Research Institute of Translational Neuroscience – DANDRITE, Nordic-EMBL Partnership for Molecular Medicine, Aarhus University
Thomas L.-M. Sørensen: Diamond Light Source, Harwell Science and Innovation Campus
Jacob Lauwring Andersen: Centre for Membrane Pumps in Cells and Disease – PUMPKIN, Danish National Research Foundation & Danish Research Institute of Translational Neuroscience – DANDRITE, Nordic-EMBL Partnership for Molecular Medicine, Aarhus University
Jens P. Andersen: Aarhus University
Charlotte Rohde Knudsen: Aarhus University
Roger B. Altman: Weill Cornell Medicine, Cornell University
Poul Nissen: Centre for Membrane Pumps in Cells and Disease – PUMPKIN, Danish National Research Foundation & Danish Research Institute of Translational Neuroscience – DANDRITE, Nordic-EMBL Partnership for Molecular Medicine, Aarhus University
Scott C. Blanchard: Weill Cornell Medicine, Cornell University

Nature, 2017, vol. 551, issue 7680, 346-351

Abstract: Abstract Phosphorylation-type (P-type) ATPases are ubiquitous primary transporters that pump cations across cell membranes through the formation and breakdown of a phosphoenzyme intermediate. Structural investigations suggest that the transport mechanism is defined by conformational changes in the cytoplasmic domains of the protein that are allosterically coupled to transmembrane helices so as to expose ion binding sites to alternate sides of the membrane. Here, we have used single-molecule fluorescence resonance energy transfer to directly observe conformational changes associated with the functional transitions in the Listeria monocytogenes Ca2+-ATPase (LMCA1), an orthologue of eukaryotic Ca2+-ATPases. We identify key intermediates with no known crystal structures and show that Ca2+ efflux by LMCA1 is rate-limited by phosphoenzyme formation. The transport process involves reversible steps and an irreversible step that follows release of ADP and extracellular release of Ca2+.

Date: 2017
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DOI: 10.1038/nature24296

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