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. 2017 Sep 15;7:11704. doi: 10.1038/s41598-017-11948-w

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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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Superposition of the internal aldimine structures of wild type AGT-Ma (early structure - gray) and S187F mutant (orange; PDB id 4I8A ref.¹⁵). Green arrows map the backbone rearrangements induced by the mutation. The main effect of the rearrangement is the new position of Lys-209 Cα that is 1.2 Å closer to the C4′ of PLP. This movement disrupts the pulling force induced by the Schiff base linkage in the wild type, uncoupling the spring mechanism. Accordingly, the residual pulling force due to the salt bridge between Asp-183 and pyridine N1 (red arrow) tilts the cofactor plane towards the re side.