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. Author manuscript; available in PMC: 2010 Nov 13.
Published in final edited form as: Cell. 2009 Nov 13;139(4):744–756. doi: 10.1016/j.cell.2009.09.034

Figure 4. Nucleotide-Dependent Motions.

Figure 4

(A) Top, (B) bottom, and side views (C-E) of the nucleotide-free and nucleotide-bound ClpX hexamers in cartoon representation following superposition. An intermediate structure obtained by averaging is also shown. For each structure, each of the six rigid-body units is a different color. Within each unit, lighter shades represent the nucleotide-free structure, intermediate shades represent the averaged structure, and darker shades represent the nucleotide-bound structure. Thus, motions induced by nucleotide binding progress from lighter to darker shades. Asymmetry of the nucleotide-free and nucleotide-bound hexamers is evident in the top and bottom views (looking along the axis of the pore) and in the side views. The views in panel B and C were generated from that in panel A by 180° and 90° rotations, respectively, around the x-axis. The views shown in panels D and E represent rotations around the y-axis in 50° and 75° increments from the view in panel C.