@article{huang_mechanism_2016,
	title = {Mechanism of {pH}-dependent activation of the sodium-proton antiporter {NhaA}},
	volume = {7},
	issn = {2041-1723},
	url = {http://www.nature.com/doifinder/10.1038/ncomms12940},
	doi = {10.1038/ncomms12940},
	abstract = {Escherichia coli NhaA is a prototype sodium-proton antiporter, which has been extensively characterized by X-ray crystallography, biochemical and biophysical experiments. However, the identities of proton carriers and details of pH-regulated mechanism remain controversial. Here we report constant pH molecular dynamics data, which reveal that NhaA activation involves a net charge switch of a pH sensor at the entrance of the cytoplasmic funnel and opening of a hydrophobic gate at the end of the funnel. The latter is triggered by charging of Asp164, the first proton carrier. The second proton carrier Lys300 forms a salt bridge with Asp163 in the inactive state, and releases a proton when a sodium ion binds Asp163. These data reconcile current models and illustrate the power of state-of-the-art molecular dynamics simulations in providing atomic details of proton-coupled transport across membrane which is challenging to elucidate by 
experimental techniques.},
	urldate = {2016-10-06},
	journal = {Nature Communications},
	author = {Huang, Yandong and Chen, Wei and Dotson, David L. and Beckstein, Oliver and Shen, Jana},
	month = oct,
	year = {2016},
	pages = {12940},
}

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