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. 2020 Apr 7;11:1727. doi: 10.1038/s41467-020-15455-x

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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. 3 — The FabF (light orange) and FabB (bright orange) interfaces can be broken up into three regions, the first two are comprised of electrostatic interactions and the third is a hydrophobic patch. The above panels provide close-up views of these three regions and the cartoon inset provides context regarding the viewing angle and the positional relationship of AcpP (cyan) to the overall AcpP–KS complex. In addition, the white hole represents the active site to which the viewed AcpP is crosslinked as the majority of contacts are provided by the KS monomer not covalently crosslinked to AcpP. a A close-up view of the AcpP–FabF region 1 electrostatic interactions. b A close-up view of the AcpP–FabF region 2 electrostatic interactions. c A close-up view of the AcpP–FabF region 3 hydrophobic interactions. d A close-up view of the AcpP–FabB region 1 electrostatic interactions. e A close-up view of the AcpP–FabB region 2 electrostatic interactions. f A close-up view of the AcpP–FabB region 3 hydrophobic interactions.