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Crystal structure of the sodium-proton antiporter NhaA dimer and new mechanistic insights


Created Date 2014-12-01
Contributor Lee, Chiara (Author) / Yashiro, Shoko (Author) / Dotson, David (ASU author) / Uzdavinys, Povilas (Author) / Iwata, So (Author) / Sansom, Mark S. P. (Author) / von Ballmoos, Christoph (Author) / Beckstein, Oliver (ASU author) / Drew, David (Author) / Cameron, Alexander D. (Author) / College of Liberal Arts and Sciences / Department of Physics
Series JOURNAL OF GENERAL PHYSIOLOGY
Type Text
Extent 16 pages
Language English
Identifier DOI: 10.1085/jgp.201411219 / ISSN: 0022-1295 / ISSN: 1540-7748
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Citation Lee, Chiara, Yashiro, Shoko, Dotson, David L., Uzdavinys, Povilas, Iwata, So, Sansom, Mark S. P., von Ballmoos, Christoph, Beckstein, Oliver, Drew, David, & Cameron, Alexander D. (2014). Crystal structure of the sodium-proton antiporter NhaA dimer and new mechanistic insights. JOURNAL OF GENERAL PHYSIOLOGY, 144(6), 529-544. http://dx.doi.org/10.1085/jgp.201411219
Note View the article as published at http://jgp.rupress.org/content/144/6/529.short
Collaborating Institutions ASU Library
Additional Formats MODS / OAI Dublin Core / RIS


  Crystal structure of the sodium-proton antiporter NhaA dimer and new mechanistic insights
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  Supplemental material
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  Video 1 - NhaA, protomer A, 0–250 ns from simulation S2/1.
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Description Stable salt-bridge network between Lys300 and Asp163/Asp164. The conformation of the network is essentially unchanged over the course of the whole simulation, and hence only the first 250 ns are shown.
  Video 2 - NhaA, protomer B, 0–250 ns from simulation S2/1.
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Description A sodium ion spontaneously binds to Asp133 and Asp164. Asp133 moves away, leaving the ion with Asp164. The salt bridge Lys300–Asp163 breaks and Asp163 binds the Na+ ion together with Asp164, preventing the reformation of the salt bridge. These interactions remain until the end of the 1-µs simulation, even though only the first 250 ns are shown.