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Figure 8. Putative substrate binding site of GTR1, GTR3, Me14g74000 and MeCGTR1.Homology modeling of GTR1, GTR3, Me14g74000 and MecGTR1 was carried out using NPF6.3 as template (see Materials and methods for details). Residues P1–13 are shown and color-coded according to legend. In blue mesh is the 3V determined central cavity (Voss and Gerstein, 2010). The inserts show P4, P5 and P6 (see text for discussion).DOI: http://dx.doi.org/10.7554/eLife.19466.026Figure 8—figure supplement 1. Alignment of glucosinolate and cyanogenic glucoside transporters with NPF6.3 and selected POT transporters.Amino acid alignment of AtGTR1, AtGTR2, AtGTR3, CpGTRL1, CpGTRL2, Me14g74000 and MeCGTR1 with NPF6.3, PepTSo, PepTSt, PepT1 (human) and PepTGk using MUSCLE (Edgar, 2004) and visualized with JalView (Waterhouse et al., 2009). Residues involved in nitrate and peptide binding are highlighted by a star and numbered P1-P15 (Doki et al., 2013; Solcan et al., 2012; Parker and Newstead, 2014; Sun et al., 2014; Newstead, 2011; Lyons et al., 2014). Helixes are indicated above the alignment and based on NPF6.3 annotation.DOI: http://dx.doi.org/10.7554/eLife.19466.027

Image published in: Jørgensen ME et al. (2017)

© 2017, Jørgensen et al. This image is reproduced with permission of the journal and the copyright holder. This is an open-access article distributed under the terms of the Creative Commons Attribution license

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