Fig. 2

In silico analysis of GH11 xylanases of Fusarium virguliforme. a F. graminearum contains amino acid substitutions that allow GH11 xylanases to escape XIP-I inhibition, including a substitution of threonine (T) to valine (V) for XylA (yellow blocks); and substitutions of asparagine (N) to cysteine (C), an insert of aspartic acid (D), and a substitution of T to C for XylB (yellow blocks). However, FvXyn11A and FvXyn11B are conserved in this region. The red block circles a string of 30 amino acids reported to induce necrosis [63]. The purple block and blue block indicate previously reported conserved residues. The name of necrosis-inducing xylanases were bold [8, 63, 64]. b Salmon color represents XIP-I. Golden color represents conserved thumb region of each xylanase. Control model of XIP-I inhibits Penicillium funiculosum GH11 xylanase XYNC. XIP-I perfectly fills into the catalyzing groove between two essential catalyzing residues glutamic acid (E) at position 85 (E85) and E176 that mimics substrates of XYNC. c The interaction between FvXyn11A and XIP-I, where the corresponding residues E114 and E205 were shown. d The interaction between FvXyn11B and XIP-I, where the corresponding residues E98 and E189 were shown