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. 2021 Jun 25;12:632685. doi: 10.3389/fgene.2021.632685

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Copyright © 2021 Faillace, Caruso, Timmers, Favero, Guzman, Rechenmacher, de Oliveira-Busatto, de Souza, Bredemeier and Bodanese-Zanettini.

This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

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Three-dimensional structure of Gma_P21. The protein structure is coloured based on its domains: (i) domain I (red), consisting of a 11 stranded β-sheet organised as a β-barrel that forms the protein core; (ii) domain II (green), consisting of an α-helix and a set of disulphide-rich loops; and (iii) domain III (blue), presenting a β-hairpin and a coil region, which are both maintained by one disulphide bond each. The main chain of the Osmotin structure is represented as cartoon and the side-chains of the residues involved in disulfide bonds are presented as yellow sticks. The Sni_SnOLP, Sni_SindOLP, Sni_Jami, Gma_OLPb, Gma_P21like, Gma_P21, Gma_OLPc, and Gma_OLPb structures share the same topology. The image was generated with PyMOL Molecular Graphics System version 1.5.0.4 (Schrödinger, LLC).