Fig. 6: The distinct loop structures determine the conformations of the holo-complexes.
From: Molecular basis for the distinct functions of redox-active and FeS-transfering glutaredoxins
a, b Comparison of the dimeric holo-complexes of the CxxC/S-type Homo sapiens Grx2 (blue, PDB 2HT9) and the CGFS-type Homo sapiens Grx5 (brown, PDB 2WUL). The alternate positions of the Fe2S2 clusters are indicated (a) as well as the rotation of the second monomer induced by the shift and rotation of the FeS cluster (b, dotted arrow). The second dimer present in the 2WUL structure was omitted for clarity. c Circular dichroism spectra of the wild-type and engineered proteins as indicated. The concentration of the FeS holo-proteins was adjusted to 175 µM using the molar absorptivity of the FeS clusters for all CD spectra recorded. Blue curves represents the proteins with the CxxC/S-type loop, brown curves the proteins with the CGFS-type loop, the gray curve Grx5 with the CSYC active site of Grx2. Source data are provided as a Source Data file.
