Fig. 1

Topology of NbXIP1;1αwt. The topology of the NbXIP1;1αwt protein showing the amino acid residues in the aromatic/arginine (ar/R) selectivity filter and the mutated residues in the NbXIP1;1α mutants. The two half helices in loops B and E are not shown in this representation. The N-terminal His₁₀-tag and the TEV protease cleavage site are in medium slate blue and violet fills, respectively. The first amino acid residue, methionine, of the NbXIP1;1αwt protein after the His₁₀-tag and the TEV protease cleavage site has been underlined. The NPA aquaporin motifs are in pale turquoise fill. The ar/R filter residues I102 (H2^P), C175 (LC^P), V242/T246 (H5^P), A257 (LE^P) and R263 (HE^P) are in crimson fill. Alternative residues, V242/T246, at the H5^P position in the ar/R filter are in blue square frame. The residue, G186, at the LC^P position in the models is in dark golden fill. L79 in helix 1 is in lime fill. Deleted residues (I165-A180) in the loop C of NbXIP1;1α mutants are in dark olive green square frame. Deleted residues (A222-K223) in the loop D of NbXIP1;1α/L79G/I102H/V242I mutants are in deep sky blue fill. Deleted residues (A222-L227) in the loop D of NbXIP1;1α/L79G/I102H/T246I mutants are in red frame. D80 in helix 1 is in blue violet fill. The topology model was created in Protter [46]