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. 2017 Jul 11;8:15957. doi: 10.1038/ncomms15957

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Copyright © 2017, The Author(s)

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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(a,b) Two tomographic slices of the same transmission electron microscopy (TEM field), from the lipid monolayer upward, showing a FtsA miniring hexagonal array (a), then aligned unbundled FtsZ protofilaments on top of the array (b) (see also Supplementary Movie 1). (c–f) A subvolume-averaged portion of a field from (a,b), with tomographic slices from the lipid monolayer (c) up to FtsZ filaments (f). (g) Segmentation of the 3D reconstructions showing potential sites of interaction where an FtsZ filament (green) intersects with the FtsA miniring (red and pink subunits). (h) Atomic structures from S. aureus FtsA (3WQU) are shown docked into the miniring densities, along with the FtsA-binding peptide from the C terminus of FtsZ (4A2A) (green) into the two subunits interacting with the crossing FtsZ protofilament. See also Supplementary Movie 2. For simplicity, the other 10 FtsZ C-terminal peptides are not shown.