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. 2017 Jul 14;7:5399. doi: 10.1038/s41598-017-05637-x

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© The Author(s) 2017

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.

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The IC interaction network that regulates the opening/closure of the IC vestibule and the transition between OF and IF states, shows distinctive dynamics in wt DAT and mutants W63A and R60A. (A) In wt DAT, the salt-bridge R60-D436 and close interactions between W63 and the F332 and Y335 stabilize substrate/sodium-binding site in the OF state. (B) In the mutant W63A, substitution of W63 by alanine breaks the stabilizing network of molecular interaction; F76 side chain dihedral angle χ ₁ rotates from ± 180° to −60°, leading to the opening of the IC vestibule. (C) Substitution of R60 by alanine breaks the salt-bridge R60-D436. Yet, alternative IC salt bridges form, such as R260-E61, which stably maintain the closed state of the IC vestibule. Residues at positions 60 and 63 are displayed in VDW format, as well as D436. In all diagrams, residues within 3 Å of W63 or W63A are shown in licorice format. Hydrated EC regions are indicated by green shaded areas.