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. 2019 Oct 22;9:15092. doi: 10.1038/s41598-019-50578-2

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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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(A) Domain organization of P-gp. HDX-MS data have been mapped on the inward-facing crystal structure of P-gp⁸. The model is colored on a rainbow scale from lowest (blue) to highest (red) by relative deuterium uptake of apo P-gp after 5 minutes of exchange. Solvent occlusion by the detergent micelle is indicated by low exchange along the transmembrane domain. (B) Diagram of the conformational transition between inward and outward-facing states. A homology model based on outward-facing MsbA was used to represent outward-facing P-gp¹¹. Structures are colored by difference in relative uptake between inward and outward-facing P-gp after 5 minutes of exchange. Regions with decreased exchange in the outward-facing state appear blue, while regions with greater exchange are colored red.