Coupled ATPase-adenylate kinase activity in ABC transporters.
Coupled ATPase-adenylate kinase activity in ABC transporters.
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DOI：
10.1038/ncomms13864
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发表时间：
2016-12-22
影响因子：
16.6
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中科院分区：
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ATP结合盒（ABC）转运蛋白是一个膜整合蛋白超家族，通过ATP水解催化底物跨膜转运。在这里，我们证明了核苷酸营业额和结合研究的基础上31 P固态NMR光谱的ABC出口商和脂质A翻转酶MsbA可以耦合ATP水解的腺苷酸激酶活性，其中ADP转化为AMP和ATP。单点突变揭示了ATP酶和腺苷酸激酶机制都与核苷酸结合结构域的相同保守基序相关。基于这些结果，我们提出了一个模型的耦合ATP酶-腺苷酸激酶的机制，涉及典型的和一个额外的核苷酸结合位点。我们将这些发现扩展到其他原核ABC出口商，即LmrA和TmrAB，这表明耦合活动是ABC出口商的一般特征。ATP结合盒（ABC）转运蛋白水解ATP以跨细胞膜转运分子。Vogel等人在此表明，ABC输出蛋白MsBA可将ATP水解与腺苷酸激酶活性偶联，该腺苷酸激酶活性似乎在低ATP水平下占主导地位，并且是ABC输出蛋白的一般特征。
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. ATP-binding cassette (ABC) transporters hydrolyse ATP to transport molecules across the cell membrane. Here Vogel et al. show that the ABC exporter MsBA can couple ATP hydrolyse to an adenylate kinase activity that seems to be predominant at low ATP levels and a general feature of ABC exporters.
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