Skip to main content
. Author manuscript; available in PMC: 2017 Mar 13.
Published in final edited form as: J Am Chem Soc. 2017 Jan 27;139(5):1900–1911. doi: 10.1021/jacs.6b11324

Figure 1. Superposition of the apo and ligand-bound forms of coproheme decarboxylase illustrate the effects of tetrapyrrole binding.

Figure 1

A. The Mn(III)-coproporphyrin-bound decarboxylase homopentamer is shown in green with the bound Mn(III)- coproporphyrin ligands as sticks (orange) (5T2K) and the ligand-free structure in yellow (1T0T). The view is down the pseudo-C5 axis with the coproheme-containing domains oriented toward the viewer. B. Superimposition of an individual subunit of coproheme decarboxylase in the apo (yellow) and ligand-bound (green) forms. Differences are localized around a flexible loop near residues 111–120 and the Mn(III)-coproporphyrin binding site. C. Close-up view of the Mn(III)-coproporphyrin binding site, illustrating prominent shifts in the positions of side chains for Asn112, Tyr113, and Arg131 in the apo- (yellow) and ligand-bound (green) forms.