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. 2018 Mar 20;9:1159. doi: 10.1038/s41467-018-03547-8

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© The Author(s) 2018

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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Fig. 4 — Modeling of C55-PP in the EcUppP active site a. Overlay of the C55-PP pyrophosphate on the observed monoolein headgroup illustrates the coordination of the pyrophosphate by the N termini of α2 and α7. b Overlay of the C55-PP on the observed monoolein headgroup highlighting the interaction network of the key catalytic residues Ser27 (nucleophile), Glu21 (base), Glu17 (carboxyl–carboxylate pair), Arg174 (coordinates beta-phosphate). c Observed coordination sphere of a bound water we propose may represent a potential binding site for the requisite catalytic cation. The overlaid pyrophosphate would contribute two ligands and a favorable electronegative stabilization to the bound metal. d Overlay of wild-type (blue) and S27A mutant (gray) crystal structures show that the active site architecture is not perturbed by the S27A mutation. To confirm the identity the S27A mutant, the wild-type model was refined against the S27A data and an mF_o-DF_c map was calculated to show the negative difference peak for the Ser27 side chain hydroxyl (contoured at 3σ)