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. 2020 Mar 27;10:5656. doi: 10.1038/s41598-020-62548-0

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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 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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Detailed PGM1 catalytic mechanism for the reversible conversion of G1P to G6P. In the substrate complex (1), the phosphate-binding loop (red) is anchoring the G1P phosphoryl group, while equatorially located hydroxyls at C3 and C4 are recognized by the sugar-binding loop (yellow). The hydroxyl group at C6 is ideally located for attack on the p-Ser phosphoryl group. After phosphoryl-transfer (2) the bisphosphorylated glucose (G16P) is poised for a 180° reorientation (“flip”) in the active site, most likely accompanied with an opening of the active site due to the flexibility of D4. Upon reorientation, G16P is again interacting with the sugar-binding loop through C3 and C4 hydroxyls, but these groups are now interchanged (3). Finally, the phosphoryl group is transferred back to the active site Ser residue on D1 (4), reactivating the PGM1 enzyme.