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. 2020 Dec 10;3:752. doi: 10.1038/s42003-020-01492-1

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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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Fig. 6 — A Top, differences in phi and psi angles between IpaH9.8^LRR-Sub and IpaH9.8^LRR-FL are shown as bar graphs. Bottom, differences in phi and psi angles between IpaH9.8^LRR-iso (PDBID: 5B0T) and IpaH9.8^LRR-FL are shown as bar graphs. Cartoons below the graphs indicate secondary structures for IpaH9.8^LRR-Sub (salmon), IpaH9.8^LRR-iso (orange), and IpaH9.8^LRR-FL (green). B Magnified view of IpaH9.8^LRR-FL (green, top-left), IpaH9.8^LRR-iso (orange, top-right) and IpaH9.8^LRR-Sub (salmon, bottom-left) near the Arg166 with backbone Cα represented as sticks. Thr165, Arg166, and Asn167 in three structures are colored red. Dashed lines indicated hydrogen bonds. Bottom-right, comparison of the main chain structures of Thr165, Arg166, and Asn167 in different IpaH9.8^LRR constructs. The main chain of Thr165, Arg166, and Asn167 are represented as sticks. Arrows indicate the main chain movement of Thr165 and Arg166 when bound to substrate. C In vitro ubiquitination assays with indicated wild-type or mutants of IpaH9.8. Reaction products were detected by CBB staining (top) and anti-hGBP1 antibody (bottom). D Magnified view of IpaH9.8^LRR-FL (green, top-left), IpaH9.8^LRR-iso (orange, top-right), and IpaH9.8^LRR-Sub (salmon, bottom-left) near Phe187, with Phe187, His210, and Tyr239 represented as sticks. Bottom-right, comparison of the LRR6 motifs in different IpaH9.8^LRR constructs with the backbone Cα shown for LRR6. The Phe187 side chain is represented as sticks. The Ca atom of Leu172, Pro173, Pro181, and Phe187 are shown as spheres. The amplifier-loops (Ser176–Asn180) in IpaH9.8^LRR-Sub and IpaH9.8^LRR-FL are indicated and colored red. Arrows indicate the main chain movement of Leu172, Pro173, Pro181, and Phe187, as well as the side chain shift of Phe187 when bound to substrate. hGBP1 is shown as both cartoon and surface (blue, bottom-left and bottom-right, respectively), with Glu110 labeled and represented as sticks. E Sequence alignment of the LRR motifs in IpaH9.8. Residues with similar properties are indicated with thin blue transparent boxes and highlighted as red. Strictly conserved residues are shown in red boxes. The amplifier loop is highlighted and in red. Leu172, Pro173, and Pro181 are conserved in LRR motifs and indicated by triangles as in D (bottom-right).