Comparison of OxsA with the characteristic HD domain dinuclear enzyme PhnZ reveals differences in the accessibility of the second metal site. Comparison.

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Comparison of OxsA with the characteristic HD domain dinuclear enzyme PhnZ reveals differences in the accessibility of the second metal site. Comparison of OxsA with the characteristic HD domain dinuclear enzyme PhnZ reveals differences in the accessibility of the second metal site. (A) The second metal site in OxsA is solvent-exposed. Ribbon drawing is shown above and space-filing model of the OxsA dimer is shown below. (B) The second metal site in PhnZ (PDB ID code 4N6W) (18) is found below the protein surface, protected by additional protein structure (labeled cap). A ribbon drawing for PhnZ is shown above and a space-filing model below. The superposition of the dinuclear sites from these two proteins is also shown with Mg2+ ions in green spheres and Fe ions in brown spheres. Jennifer Bridwell-Rabb et al. PNAS 2016;113:48:13750-13755 ©2016 by National Academy of Sciences