Crystal structures reveal the molecular basis of ion translocation in sodium/proton antiporters. Coincon, M., Uzdavinys, P., Nji, E., Dotson, D. L., Winkelmann, I., Abdul-Hussein, S., Cameron, A. D., Beckstein, O., & Drew, D. Nature Structural & Molecular Biology, 23(3):248–255, March, 2016.
Crystal structures reveal the molecular basis of ion translocation in sodium/proton antiporters [link]Paper  doi  abstract   bibtex   
To fully understand the transport mechanism of Na+/H+ exchangers, it is necessary to clearly establish the global rearrangements required to facilitate ion translocation. Currently, two different transport models have been proposed. Some reports have suggested that structural isomerization is achieved through large elevator-like rearrangements similar to those seen in the structurally unrelated sodium-coupled glutamate-transporter homolog GltPh. Others have proposed that only small domain movements are required for ion exchange, and a conventional rocking-bundle model has been proposed instead. Here, to resolve these differences, we report atomic-resolution structures of the same Na+/H+ antiporter (NapA from Thermus thermophilus) in both outward- and inward-facing conformations. These data combined with cross-linking, molecular dynamics simulations and isothermal calorimetry suggest that Na+/H+ antiporters provide alternating access to the ion-binding site by using elevator-like structural transitions.
@article{coincon_crystal_2016,
	title = {Crystal structures reveal the molecular basis of ion translocation in sodium/proton antiporters},
	volume = {23},
	copyright = {© 2016 Nature Publishing Group, a division of Macmillan Publishers Limited. All Rights Reserved.},
	issn = {1545-9993},
	url = {http://www.nature.com/nsmb/journal/v23/n3/full/nsmb.3164.html},
	doi = {10.1038/nsmb.3164},
	abstract = {To fully understand the transport mechanism of Na+/H+ exchangers, it is necessary to clearly establish the global rearrangements required to facilitate ion translocation. Currently, two different transport models have been proposed. Some reports have suggested that structural isomerization is achieved through large elevator-like rearrangements similar to those seen in the structurally unrelated sodium-coupled glutamate-transporter homolog GltPh. Others have proposed that only small domain movements are required for ion exchange, and a conventional rocking-bundle model has been proposed instead. Here, to resolve these differences, we report atomic-resolution structures of the same Na+/H+ antiporter (NapA from Thermus thermophilus) in both outward- and inward-facing conformations. These data combined with cross-linking, molecular dynamics simulations and isothermal calorimetry suggest that Na+/H+ antiporters provide alternating access to the ion-binding site by using elevator-like structural transitions.},
	language = {en},
	number = {3},
	urldate = {2016-04-04},
	journal = {Nature Structural \& Molecular Biology},
	author = {Coincon, Mathieu and Uzdavinys, Povilas and Nji, Emmanuel and Dotson, David L. and Winkelmann, Iven and Abdul-Hussein, Saba and Cameron, Alexander D. and Beckstein, Oliver and Drew, David},
	month = mar,
	year = {2016},
	keywords = {Membrane proteins, X-ray crystallography},
	pages = {248--255},
}
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