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. 2017 Aug 15;8:263. doi: 10.1038/s41467-017-00361-6

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© The Author(s) 2017

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 — Model of functional amyloid secretion in Pseudomonas. Fap components are secreted through the inner membrane (IM) via the Sec pathway. FapB (blue), FapC (red) and FapE (magenta) remain unfolded in the periplasm. FapF (grey) forms a stable trimer within the outer membrane (OM). The N-terminal coiled-coil of FapF resides in the periplasm. Conformational change of one or more FapF ‘plug’ domains allows substrate secretion through the OM. For simplicity we show a single plug (purple) motion here. FapD (green) proteolytic activity essential for secretion. Two suggested models for the architecture of FapE, FapB and FapC in fibres on the extracellular surface of the OM