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. 2020 Jun 8;11:2877. doi: 10.1038/s41467-020-16511-2

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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. 1 — a P140 contains a large N-terminal domain and a smaller C-terminal domain, which is followed in sequence by a predicted transmembrane helix. The N-terminal domain has two distinct regions: the β-propeller (green) and the crown (blue). b Two views of the β-propeller, 70° apart. The first and last β-sheets of the propeller (I and VII, respectively) interact with the C-terminal domain and are structurally contiguous in the propeller ring. A large β-bulge (residues 69–77, in cyan) occludes the center of the propeller ring. The presence of only two strands in the last β-sheet (VII) constrains the interface between the N-terminal and C-terminal domains.