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. 2021 Jun 23;11:13172. doi: 10.1038/s41598-021-92604-2

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© The Author(s) 2021

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 licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence 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 licence, visit http://creativecommons.org/licenses/by/4.0/.

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Comparison of crystal structures of VdesOBP1 with the closest related OBPs from Phormia regina (PregOBP56) and Leucophera madereae (LmadPBP). (a) Ribbon view of the superposition of monomers from VdesOBP1 (rainbow coloured) and PregOBP56 (light grey) with its two fatty acid ligands (grey sticks). Note the absence of the classical OBP fold helix 2 (red squared) in VdesOBP1. (b) Ribbon view of the superposition of monomers from VdesOBP1 (rainbow coloured) and LmadPBP. Note the absence of the classical OBP fold helix 2 (red squared) in VdesOBP1 as compared to LmadPBP (red squared) and the shift of one disulphide bridge (red arrow). The 3D positions of the two other disulphide bridges are conserved (purple arrow), in the final fold, although as result of different C1-C6, C2-C3, C4-C5 (VdesOBP1) and C1-C3, C2-C5, C4-C6 (LmadPBP) connectivities. Figure made with PyMOL (version 1.5.0.2. http://www.pymol.org).