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. Author manuscript; available in PMC: 2016 Dec 24.
Published in final edited form as: Methods Enzymol. 2016 Jun 24;580:223–250. doi: 10.1016/bs.mie.2016.05.009

Figure 2.

Figure 2

Application of MDPSA to the natively monomeric cyt cb562 (PDB ID: 2BC5), giving the MBPC1 metalloprotein scaffold. In the crystal lattice, cyt cb562 forms extensive packing interactions along Helix 3 (residues 56-81), which was chosen as the surface to install two bis-His clamps (H59/H63 & H73/H77). MBPC1 forms three distinct metal-bound oligomers dictated by the stereochemical preferences of the metal ions: a Ni-bound trimer (PDB ID: 3DE9), a Cu-bound dimer (PDB ID: 3DE8), and a Zn-bound tetramer (PDB ID: 2QLA). Metal ligands are shown as sticks and metal ions are shown as spheres. Close-up images show the metal coordination environments: Ni2+ is coordinated either by three H59/H63 (shown) or three H73/H77 bis-His clamps from three different protomers. Cu2+ is coordinated by H59, H63, H73' and H77' from two different protomers. Zn2+ is coordinated by H63, H73', H77' and D74” from three different protomers.