Table 2.
Distance between the residue mutated in XylE to xylose (DtX) in Angstrom (Å) and the binding energies (kcal/mol) of Cs4130, Gxf1, XylE and variants complexed to xylose through molecular docking analysis
| XylE | Cs4130 | Gxf1 | DtX (Å) | |
|---|---|---|---|---|
| Residue (kcal/mol) | ||||
| Wild-type | − 27.4 | − 28.8 | − 26.0 | – |
| Mut1 | F24A (− 27.6/0.2) | F58A (− 27.8/1.0) | F58A (24.9/1.1) | 3.9 |
| G83A | G120A | G120A | 22.0 | |
| R133C | R153C | R153C | 11.7 | |
| E153A | E173A | E173A | 17.8 | |
| R160A | R180A | R180A | 14.3 | |
| Mut 2 | Q168A (− 28.3/0.9) | Q188A (− 26.4/2.4) | Q188A (− 25.5/0.5) | 2.3 |
| Mut 3 | Q288A (− 26.4/1.0) | Q314A (− 28.1/0.7) | Q314A (− 24.9/1.1) | 2.9 |
| Mut 4 | Q289A (− 26.6/0.8) | Q315A (− 28.5/0.3) | Q315A (− 26.1/0.1) | 3.0 |
| Mut 5 | N294A (− 28.1/0.7) | N320A (− 28.2/0.6) | N320A (− 25.2/0.8) | 2.9 |
| Mut 6 | Y298A (− 26.4/1.0) | Y324A (− 28.1/0.7) | Y324A (− 25.8/0.2) | 4.3 |
| Mut 7 | N325A (− 27.4/0) | N349A (− 26.9/1.9) | N349A (− 25.7/0.3) | 6.7 |
| G340A | G364A | G364A | 15.8 | |
| R341A | R365A | R365A | 14.3 | |
| Mut 8 | W392A (− 26.6/0.8) | Y428A (− 27.9/0.9) | Y431A (− 25.6/0.7) | 3.1 |
| E397A | E433A | E436A | 14.2 | |
| R404A | K440A | R443A | 16.1 | |
| Mut 9 | Q415A (− 26.8/0.6) | N451A (− 28.0/0.8) | N454A (− 26.6/0.6) | 2.7 |
| Mut 10 | W416A (26.5/0.9) | W452A (− 28.5/0.3) | W455A (− 25.4/0.6) | 4.8 |
Residues close and far from ligand (xylose) are highlighted in italics and underlined, respectively
The energy of binding (kcal/mol) of mutants and the difference from the wild-type are between parentheses
Mut mutant