Figure 8

Identification of a convergent heme binding surfaces from surface similarity. Despite lacking sequence or structural homology to the heme-monooxygenase family, IsdG from S. aureus (a, yellow) contains a conserved surface allowing it to perform heme-monooxygenase activity. When compared to the heme binding surface from heme oxygenase (HmuO) from C. diphtheria (b, green), 19 residues are conserved (c) with similar global shape characteristics (d). The superposition of the conserved residues is shown for the best scoring cRMSD (e) and oRMSD (g) alignments. The alignments are colored by residue type (IsgG large radius, HmuO small radius) in (fh). The superposition of the surfaces resulting in the maximum volume overlap (i, red) is shown with bound heme from HmuO (j).