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. 2018 Feb 22;8:3489. doi: 10.1038/s41598-018-21631-3

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© The Author(s) 2018

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) 3D models of putative Mayetiola destructor (Mdes) Orco tetra- and pentamers, viewed from the extracellular surface. (b) Putative tetramer model of MdesOrco multimer, viewed from extracellular surface, with selected residues shown in sphere representation. Blue (H81F), green (N133L) and gold (S350A) spheres represent MdesOrco residues mutated in this study. Grey spheres represent corresponding residues associated with cation selectivity or ion channel function; tan spheres represent residues associated with ligand binding³⁴. (c) Side view of MdesOrco tetramer with selected residues shown in sphere representation as described in (b). Note: protein models are coloured from blue (N-termini) to red (C-termini).