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. 2017 Aug 3;7:7234. doi: 10.1038/s41598-017-06973-8

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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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Conformational changes enforce changes in coordinating residues in the Mn active site. (a) The ligand-free structure shows Mn coordinated to a water, His150, His175, and Asp153 (all deriving from the α-subunit). The Mn-proximal α-helix is structured, blocking the Mn site from access to the α/β interface and solvent. (b) The AMP-bound structure shows Mn coordinated to His150, His175, Asp153, and Glu89. Nucleotide binding to the β subunit induces large conformational changes that cause the Mn-proximal α-helix to form a disordered loop, allowing the Glu89 side chain to coordinate to the Mn site. (c) Acetate-bound structure shows the displacement of Glu89 and the concomitant reorganization of the Mn-proximal α-helix. The internal channel is closed and the substrate-access channel is open in this structure, which is proposed to illustrate the effects of displacement of Glu89 from the Mn by phosphorylated intermediates.