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. Author manuscript; available in PMC: 2008 Nov 2.
Published in final edited form as: J Mol Biol. 2007 Aug 23;373(4):1006–1016. doi: 10.1016/j.jmb.2007.08.040

Figure 6.

Figure 6

Cartoon representation of the structural alignment of the free, substrate-bound and product-bound forms of human ferrochelatase. (a) Cartoon overlay of the wild-type, substrate-free structure in cream color. Areas of significant movement are highlighted in color. The upper lip of the active site that is altered in spatial orientation in the E343K substrate-bound variant relative to the wild-type enzyme structure is shown in green. The unwound π helix segment of the F110A product-bound variant enzyme is shown in red. Bound protoporphyrin IX is shown in brick and highlighted using dots to denote the electron density. The [2Fe-2S] cluster is shown as yellow and blue spheres. (b) Enlarged view of the bound protoporphyrin IX (brick) and bound heme (purple) in the same spatial orientation as shown in the cartoon model. The movement of the protoporphyrin/protoheme IX propionate 6, which is on the corner of the macrocycle in this orientation, is highlighted by the grey arrow.