A comparative structural analysis of the surface properties of asco-laccases
Fig 7
Conservation of glycosylation and surface residues between asco-laccases.
A)- D) Surface representations of MtL color-coded according to domains and showing the distribution of glycans around the protein. Glycosylation seen in the MtL crystal structure are shown as orange sticks together with the numbering of the anchoring Asn residues. E)- H) Surface representations of MtL with mapping of sequence conservation according to the MSA in Fig 4. Residues that are fully conserved among all five asco-laccases with known structures (MtL, MaL, TaL, BaL and AnL) are shown in dark blue (including conservative substitutions Arg/Lys and Asp/Glu). Additional residues that are only conserved within the MtL-MaL-TaL subgroup, but not in BaL and/or AnL, are mapped in light blue. Ligands from 3FU7 (2,6-DMP black) and 4YVN (ABTS cyan) are shown as space-filling molecules to indicate the location of the T1-substrate binding pocket and putative ABTS-site, respectively. Surface areas corresponding to the MtL dimer interface and the entry/exit of the T2-solvent channel are indicated with dashed green lines.