Figure 1: Crystal structure of the RACo:CoFeSP complex.
From: ATP-induced electron transfer by redox-selective partner recognition
(a) Overall structure in cartoon and surface representation. The small (CfsB) and large (CfsA) subunit of CoFeSP are shown in yellow and blue, respectively. The RACo dimer is coloured in pink tones. The [4Fe4S] clusters of CoFeSP are illustrated as spheres in yellow (sulphur) and orange (iron). The cobalamin cofactor is depicted as cyan spheres. (b) Domain movements within CoFeSP. The structures of free CoFeSP (red, PDB 2YCL)12 and CoFeSP in the RACo:CoFeSP complex (blue) are superimposed on the small subunit CfsB (grey) to illustrate the domain movements in CfsA. A green (free CoFeSP) and an orange (complex) arrow indicate the distances between the [4Fe4S] cluster and the cobalamin cofactor. Black arrows point to the displacement of the cofactor-binding domains.
