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. 2022 Sep 24;13:5603. doi: 10.1038/s41467-022-33379-6

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© The Author(s) 2022

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 — A The structure of Pfs48/45 taken from that of full-length Pfs48/45 bound to 10D8, viewed from two different directions. The N-terminal (D1), central (D2) and C-terminal domains (D3) are light, medium and dark blue. The right-hand panel also indicates the membrane and the 20 residue long linker not included in our constructs. B Comparison of the three full-length Pfs48/45 structures. Three structures were constructed by taking the models of Pfs48/45 from the three different crystal structures of Pfs48/45 bound to different antibody combinations and aligning the structure of the N-terminal domain onto the fragments of the domain built into the electron density. These composite structures have been aligned based on the central and C-terminal domains, showing the motion of the N-terminal domain, highlighted by the red arrow. C Histogram showing the observed interdomain angles in full-length Pfs48/45 during atomistic molecular dynamics simulations. To define these angles two lines were drawn, linking the centres of mass of the N-terminal and central domains and those of the central and C-terminal domains. The angle shown is that between these lines. The three coloured histograms refer to outcomes of three independent simulations which started with the models in panel (B) with histograms being constructed by pooling five replicates for each starting structure. The black histogram is the pooled distribution of all replicates in all three starting models. D The average angle observed in the simulations from (C). is shown top-centre with the most closed observed model bottom-left and the most open model bottom-right. Red lines are as described in C. E shows the fitting of models from the molecular dynamic simulations to data from small angle X-ray scattering. Each point represents a different model and the χ² gives the quality of fit to the scattering curve. Horizontal lines show the χ² for the fit corresponding to interdomain angles found in the three crystal structures, as seen in B.