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Coupled ATPase-adenylate kinase activity in ABC transporters.


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.

SUBMITTER: Kaur H 

PROVIDER: S-EPMC5192220 | biostudies-literature | 2016 Dec

REPOSITORIES: biostudies-literature

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Coupled ATPase-adenylate kinase activity in ABC transporters.

Kaur Hundeep H   Lakatos-Karoly Andrea A   Vogel Ramona R   Nöll Anne A   Tampé Robert R   Glaubitz Clemens C  

Nature communications 20161222


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 <sup>31</sup>P 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  ...[more]

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