Figure 2. Doc sequences used in this study (N- to C-terminus).
Doc_wt: wild-type sequence; hydrophobicity and charge graphs are displayed for the wild-type-Doc (red: positively charged, blue: negatively charged); (GS)x8_insert: A (Gly-Ser)8 linker was incorporated between helix 1 and helix 2; Q1_mutant: Quadruple mutant in helix 1. Four point mutations (DE/AA) were incorporated into Doc helix 1 to knock out binding mode A; Q3_mutant: Quadruple mutant in helix 3. Four point mutations (DE/AA) were incorporated into Doc helix 3 to knock out binding mode B; QQ_mutant: Non-binding control with both binding modes knocked out. Numbers below indicate amino acid number of the fusion protein construct starting from the xylanase N-terminus.