Figure 4.

Structural comparisons of Ao(AA11) with known AA9 and AA10 enzymes. (a) 3D structure of Cu-Ao(AA11), ribbon depiction. The conserved active site residues are shown as sticks with green carbons and disulfide bonds (from conserved cysteines) as yellow sticks. (b) Overall superposition of Cu-Ao(AA11) (green) with Zn-(AA9) from T. terrestris (yellow) with rmsd = 2.6 Å over 145 Cα’s (c) Superposition of Cu-Ao(AA11) (green) with Cu-(AA10) from E. faecaelis (pink) with r.m.s.d = 2.3 Å over 118 residues overlapping with a Cα’s. (d) The electron density maps contoured at 1σ in the active site of Cu-Ao(AA11), Cu-N(His 1) = 1.97 Å, Cu-NH₂(His1) = 2.19 Å, Cu-N(His60) = 1.98 Å, N(His1)-Cu-NH₂ = 90.5°, N(His60)-Cu-NH₂ = 103.0°, N(His1)-Cu-N(His1) = 164.8°. Glu74, marked with asterisk is from a symmetry related molecule and is shown with yellow carbon atoms. (e) Active site overlay of Ao(AA11) (green carbons/copper) with Cu-AA9 from T. aurantiacus (orange carbons/copper), note side chain of conserved alanine 58, depicted as green rod in AA11. (f) The active site overlap of Cu-Ao(AA11) (green carbons/copper) with Cu-(AA10) from B. amyloliquefaciens (pink carbons/copper). See Supplementary figure 5 for stereo views of d-f.