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Coupled ATPase-adenylate kinase activity in ABC transporters

Author

Listed:
  • Hundeep Kaur

    (Institute for Biophysical Chemistry and Centre for Biomolecular Magnetic Resonance, Goethe-University Frankfurt)

  • Andrea Lakatos-Karoly

    (Institute for Biophysical Chemistry and Centre for Biomolecular Magnetic Resonance, Goethe-University Frankfurt)

  • Ramona Vogel

    (Institute for Biophysical Chemistry and Centre for Biomolecular Magnetic Resonance, Goethe-University Frankfurt)

  • Anne Nöll

    (Institute for Biochemistry, Goethe-University Frankfurt)

  • Robert Tampé

    (Institute for Biochemistry, Goethe-University Frankfurt)

  • Clemens Glaubitz

    (Institute for Biophysical Chemistry and Centre for Biomolecular Magnetic Resonance, Goethe-University Frankfurt)

Abstract

ATP-binding cassette (ABC) transporters, a superfamily of integral membrane proteins, catalyse the translocation of substrates across the cellular membrane by ATP hydrolysis. Here we demonstrate by nucleotide turnover and binding studies based on 31P solid-state NMR spectroscopy that the ABC exporter and lipid A flippase MsbA can couple ATP hydrolysis to an adenylate kinase activity, where ADP is converted into AMP and ATP. Single-point mutations reveal that both ATPase and adenylate kinase mechanisms are associated with the same conserved motifs of the nucleotide-binding domain. Based on these results, we propose a model for the coupled ATPase-adenylate kinase mechanism, involving the canonical and an additional nucleotide-binding site. We extend these findings to other prokaryotic ABC exporters, namely LmrA and TmrAB, suggesting that the coupled activities are a general feature of ABC exporters.

Suggested Citation

  • Hundeep Kaur & Andrea Lakatos-Karoly & Ramona Vogel & Anne Nöll & Robert Tampé & Clemens Glaubitz, 2016. "Coupled ATPase-adenylate kinase activity in ABC transporters," Nature Communications, Nature, vol. 7(1), pages 1-13, December.
    • Handle: RePEc:nat:natcom:v:7:y:2016:i:1:d:10.1038_ncomms13864
    DOI: 10.1038/ncomms13864
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    Cited by:

    1. Jixing Lyu & Chang Liu & Tianqi Zhang & Samantha Schrecke & Nicklaus P. Elam & Charles Packianathan & Georg K. A. Hochberg & David Russell & Minglei Zhao & Arthur Laganowsky, 2022. "Structural basis for lipid and copper regulation of the ABC transporter MsbA," Nature Communications, Nature, vol. 13(1), pages 1-11, December.
    2. Takeshi Tsunoda & Arash Samadi & Sachin Burade & Taifo Mahmud, 2022. "Complete biosynthetic pathway to the antidiabetic drug acarbose," Nature Communications, Nature, vol. 13(1), pages 1-12, December.

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