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. 2014 Mar 18;9(3):e92089. doi: 10.1371/journal.pone.0092089

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© 2014 Heinzelmann, Kuyucak

This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited.

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(A) Glutamate substrate (in green) bound to EAAT3 in the closed outward state with a protonated E374 side chain. (B) The same but with a deprotonated E374 side chain. Glutamate is stable in A for 20 ns, but becomes unstable in B, losing most of the contacts after 10 ns of simulations.