A comparative structural analysis of the surface properties of asco-laccases
Fig 4
Structure-based alignment of MtL, MaL (2Q9O), TaL (3PPS), BaL (3QSR) and AnL (5LM8).
Structural features of particular interest in this study, such as glycosylation, dimer interface and MtL variants, are indicated above the alignment. For MtL, the putative consensus sites for N-glycosylation (N-x-T/S) are shown as orange triangles. The triangles are filled at the positions where glycan was observed in the structure. Residues located at the interface of the MtL dimer are indicated with an “i”. MtL variants discussed in the paper are denoted with blue triangles. Conserved secondary structure elements, domains, Cu-ligands and the residues forming the T1-pocket are shown below the alignment. β-Strands are color-coded corresponding to the three domains (A residues 1–161 blue, B residues 162–341 green and C residues 342–559 yellow) as in the Fig 3. Cu-ligands are represented with orange circles. Open circles indicate hydrophobic ligands like Leu513. Hydrophobic residues that line the T1-pocket, based on the MaL:2,6-DMP complex [8], are indicated with black dots while His508 and Glu235, which form the polar recognition motif, are shown as blue and red dots, respectively. The extra polar residue, Glu497, in the T1-pocket of BaL (and AnL) is indicated with a green dot. Note that the N-terminal region of the AnL structure is disordered and the residue numbers for AnL in the MSA must be corrected (+27) to match the numbering in the mature enzyme sequence.