Skip to main content
. Author manuscript; available in PMC: 2011 May 12.
Published in final edited form as: Structure. 2010 May 12;18(5):553–562. doi: 10.1016/j.str.2010.02.016

Figure 3.

Figure 3

Pseudo-atomic model of the ClpA hexamer. The D1 (A) and D2 (B) tiers were built separately. Each monomer is colored differently. A and B show axial views looking from ClpA towards ClpP. The arrows in A and B point to two segments of ClpA lying outside the EM density; the segment in A corresponds to an α-helix linked to the sensor 1 motif and that in B to the D2 diaphragm loop (for clarity, only one loop from the red monomer is shown). Panel C shows a side view, the unoccupied density (black oval) corresponds to the location of the 10 amino acid linker between D1 and D2 that is not shown. Residues 610 and 628 (marked) are the two ends of the ClpA motif that interacts with ClpP. The model places these two residues in the immediate vicinity of the bump of unoccupied ClpP density shown at the bottom of the panel.