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. 2020 Nov 29;25(23):5619. doi: 10.3390/molecules25235619

Figure 3.

Figure 3

Structural basis of hetero-transglycosylation reactions catalysed by plant XETs with neutral acceptor substrates. (A) sequence alignment of specific and nonspecific XETs to indicate target residues destined for mutagenesis in TmXET6.3 to suppress the hetero-transglycosylation activity with neutral acceptors (blue, mutations H94Q and Q108R) and evoke the hetero-transglycosylation activity with the charged [α(1-4)GalAp]5 acceptor (green, mutations W75H, Y110R). Red asterisks mark catalytic residues [125]; (B) superposition of poplar PttXET16A (PDB accession 1UN1; red) and the TmXET6.3 model [123] orange; points to differences in residues between the two structures, which are visualised in yellow (PttXET16A) and black (TmXET6;3) sticks; (C) interactions of the XXXG acceptor (cpk green) with the residues of PttXET16A (yellow sticks) and TmXET6.3 (black sticks); (D) Venn diagram of the occurrence of nonspecific XETs (with detailed residue configurations) based on the analysis of 3394 UniProtKB entries [123].