Coupled ATPase-adenylate kinase activity in ABC transporters

Hundeep Kaur, Andrea Lakatos-Karoly, Ramona Vogel, Anne Nöll, Robert Tampé and Clemens Glaubitz ()
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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

Nature Communications, 2016, vol. 7, issue 1, 1-13

Abstract: 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.

Date: 2016
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DOI: 10.1038/ncomms13864

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