The ins and outs of vanillyl alcohol oxidase: Identification of ligand migration paths
Fig 10
Overview of the identified paths and the ligands proposed to migrate through them (uni-or bi-directional).
The VAO dimer is shown in surface representation, with the cap domain coloured in red and the FAD-binding domain coloured in green and the FAD cofactor shown as sticks in yellow. Coloured arrows indicate the paths for phenolic ligands (cap path in orange, FAD path in blue and subunit interface path in magenta). Filled in arrowheads indicate paths to the si side of FAD and empty arrowheads paths to the re side of FAD. Drawn out lines indicate the path is on the side of VAO facing the viewer, and dotted lines indicate the path is on the back side of VAO. Note that the two subunits are rotated 180 degrees relative to each other in the VAO dimer and that a path pointing towards the viewer in the right monomer is pointing away from the viewer in the left monomer and vice versa. The location of the concierge residues, His466 and Tyr503, is represented by a black line. The portal formed by Met192, Met195 and Glu464 is indicated by an ellipse. The bottlenecks formed by Arg312 and Arg398 in the cap path and Trp89 and Lys5454 in the FAD path are represented by pentagrams and heptagrams, respectively.