Fig. 6.

Comparison of RPE65 with ACO. (A) Selected residues of RPE65 are plotted to equivalent positions on the carbon backbone of the ACO crystal structure (22) by using the visual molecular dynamics program (Version 1.8.3; www.ks.uiuc.edu/Research/vmd) (42). Residues are iron-coordinating (blue), conserved residues associated with disease (pink), conserved/nonconserved cysteines (yellow), and weak pathogenic/nonpathogenic mutations (red). The iron-coordinating residues are clustered in the proposed substrate binding tunnel. Residues more sensitive to mutation tend to occur in the core. (B) Sequence alignment of RPE65 and ACO showing key iron-coordinating, cysteine, and other residues. The original alignment obtained with DeepView/Swiss-PdbViewer (Version 3.7; http://ca.expasy.org/spdbv) was manually adjusted to maximize gap suppression and alignment with predicted structural features (β-sheets and α-helices). Residues are color-coded as above. ^*, identity; ·, similarity.