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. 2019 Jul 25;10:3315. doi: 10.1038/s41467-019-11322-6

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© The Author(s) 2019

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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Fig. 4 — MD simulations and mutational analysis of MerMAID1. a Overview of the MD simulation homology model of MerMAID1 in the dark. The predicted ion permeation pathway is shown as mesh (b1, b2), and ribbons represent the protein backbone. b Electrostatic surface potential of the predicted chloride permeation pathway. c Detailed view of the active-site residues, with amino acids shown as cyan sticks and the all-trans retinal (ATR) in orange. Red spheres denote water molecules that remained stable during MD simulation. d Representative photocurrent traces of wild-type (WT) MerMAID1 and selected MerMAID1 mutants recorded at −60 mV. Photocurrent amplitudes (e), λ_max (f), apparent τ_des of the peak current (g), recovery time constant, τ_rec (h), and extent of desensitization (i) of WT MerMAID1 and indicated mutants. Mean values (thick lines) ± standard deviation (whiskers) are shown, and single-measurement data points are represented as dots. Source data are provided as a Source Data file (e–i)