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Structure and mechanism of Zn2+-transporting P-type ATPases

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  • Kaituo Wang

    (Centre for Membrane Pumps in Cells and Disease (PUMPkin), Danish National Research Foundation, Aarhus University, Gustav Wieds Vej 10C, DK-8000 Aarhus C, Denmark
    Present addresses: Department of Biomedical Sciences, University of Copenhagen, Blegdamsvej 3B, DK-2200 Copenhagen, Denmark (K.W. and P.G.); Department of Experimental Medical Science, Lund University, Sölvegatan 19, SE-221 84 Lund, Sweden (P.G.).)

  • Oleg Sitsel

    (Centre for Membrane Pumps in Cells and Disease (PUMPkin), Danish National Research Foundation, Aarhus University, Gustav Wieds Vej 10C, DK-8000 Aarhus C, Denmark)

  • Gabriele Meloni

    (Centre for Membrane Pumps in Cells and Disease (PUMPkin), Danish National Research Foundation, Aarhus University, Gustav Wieds Vej 10C, DK-8000 Aarhus C, Denmark)

  • Henriette Elisabeth Autzen

    (Centre for Membrane Pumps in Cells and Disease (PUMPkin), Danish National Research Foundation, Aarhus University, Gustav Wieds Vej 10C, DK-8000 Aarhus C, Denmark)

  • Magnus Andersson

    (Science for Life Laboratory, Swedish e-Science Research Center, KTH Royal Institute of Technology, SE-171 21 Solna, Sweden)

  • Tetyana Klymchuk

    (Centre for Membrane Pumps in Cells and Disease (PUMPkin), Danish National Research Foundation, Aarhus University, Gustav Wieds Vej 10C, DK-8000 Aarhus C, Denmark)

  • Anna Marie Nielsen

    (Centre for Membrane Pumps in Cells and Disease (PUMPkin), Danish National Research Foundation, Aarhus University, Gustav Wieds Vej 10C, DK-8000 Aarhus C, Denmark)

  • Douglas C. Rees

    (California Institute of Technology, 1200 East California Boulevard, Pasadena, California 91125, USA)

  • Poul Nissen

    (Centre for Membrane Pumps in Cells and Disease (PUMPkin), Danish National Research Foundation, Aarhus University, Gustav Wieds Vej 10C, DK-8000 Aarhus C, Denmark)

  • Pontus Gourdon

    (Centre for Membrane Pumps in Cells and Disease (PUMPkin), Danish National Research Foundation, Aarhus University, Gustav Wieds Vej 10C, DK-8000 Aarhus C, Denmark
    Present addresses: Department of Biomedical Sciences, University of Copenhagen, Blegdamsvej 3B, DK-2200 Copenhagen, Denmark (K.W. and P.G.); Department of Experimental Medical Science, Lund University, Sölvegatan 19, SE-221 84 Lund, Sweden (P.G.).)

Abstract

The X-ray crystal structures of a zinc-ion-transporting P-type ATPase are solved in a zinc-free, phosphoenzyme ‘ground’ state and in a transition state of dephosphorylation, characterizing these transporters of an essential micronutrient that is needed for many biological processes but is cytotoxic when free.

Suggested Citation

  • Kaituo Wang & Oleg Sitsel & Gabriele Meloni & Henriette Elisabeth Autzen & Magnus Andersson & Tetyana Klymchuk & Anna Marie Nielsen & Douglas C. Rees & Poul Nissen & Pontus Gourdon, 2014. "Structure and mechanism of Zn2+-transporting P-type ATPases," Nature, Nature, vol. 514(7523), pages 518-522, October.
    • Handle: RePEc:nat:nature:v:514:y:2014:i:7523:d:10.1038_nature13618
    DOI: 10.1038/nature13618
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    Cited by:

    1. Yves-Marie Boudehen & Marion Faucher & Xavier Maréchal & Roger Miras & Jérôme Rech & Yoann Rombouts & Olivier Sénèque & Maximilian Wallat & Pascal Demange & Jean-Yves Bouet & Olivier Saurel & Patrice , 2022. "Mycobacterial resistance to zinc poisoning requires assembly of P-ATPase-containing membrane metal efflux platforms," Nature Communications, Nature, vol. 13(1), pages 1-17, December.
    2. Nina Salustros & Christina Grønberg & Nisansala S. Abeyrathna & Pin Lyu & Fredrik Orädd & Kaituo Wang & Magnus Andersson & Gabriele Meloni & Pontus Gourdon, 2022. "Structural basis of ion uptake in copper-transporting P1B-type ATPases," Nature Communications, Nature, vol. 13(1), pages 1-11, December.

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