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. 2020 Oct 9;10:16903. doi: 10.1038/s41598-020-73906-3

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© The Author(s) 2020

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 licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence 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 licence, visit http://creativecommons.org/licenses/by/4.0/.

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Influence of KDEL-binding upon water pockets (a) Apo state (green cartoon) there are two large fully-solvated pockets to the lumenal (grey) and cytoplasmic sides (orange). They are almost, but not quite, connected. (b) Upon binding of KDEL the conformational changes in the protein (cyan cartoon) result in the shrinkage of both original water pockets and the formation of an additional pocket between E127 and Y191 (red). (c) Summarises the key conformational changes that occur when moving from the Apo (green) to KDEL-bound state (cyan). Y151 extends into the water pocket (orange surface in a,b), reducing its size while Y191 retracts away to help the formation of the new water pocket (red surface in b). (d) KDEL binding creates a zone of ordered waters, where the largest cavity is occupied by two waters surrounded by a hydrophobic pocket formed from I124, W166 and A180.