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. Author manuscript; available in PMC: 2015 Apr 3.
Published in final edited form as: Structure. 2012 Mar 7;20(3):545–553. doi: 10.1016/j.str.2012.01.018

Figure 2.

Figure 2

Crystal structure of P. furiosus Cmr2dHD. (A) Overview and domain structure of Cmr2dHD. Cmr2dHD is a flat, triangular, four-domain protein. The N-terminal domain D1 (blue) contains a ferredoxin-like fold (which contains a P-loop) and a cysteine cluster. The D3 domain (orange) contains a ferredoxin fold that includes a conserved GGDD motif on a β-hairpin and a P-loop structure. Domains D2 (green) and D4 (red) are exclusively α-helical. (B) Topology of the Cmr2dHD structure with the same coloring scheme as panel A. Arrows represent β-sheets and cylinders represent α-helices. Dashed lines represent disordered regions. The P-loops of D1 and D3, the β-hairpin of D3 and the cysteine cluster of D1 are indicated. (C) Cmr2dHD contains two homologous ferredoxin folds (colored in blue and orange for the D1 and D3 domains respectively). The D1 ferredoxin-like fold lacks the β-hairpin but maintains the P-loop (purple). The D3 domain contains both the β-hairpin (yellow) and P-loop (purple). (D) D1 and D3 domains are homologous. The two domains have a root-means-square-deviation of 2.6 Å. (E) Electrostatic surface potential of Cmr2dHD bound with adenosine diphosphate (ADP). See also Figure S4.