Figure 5 - full size

 

Figure 5.
Figure 5. The N-terminal domain rotates to accommodate compression of the RecA filament. a, Two neighboring monomers in the RecA filament are shown in yellow and cyan in an orientation similar to that of the subunits on the front of the filaments shown in Figure 2. This orientation is chosen to optimize the visibility of the monomer-monomer interaction. Form 1 (PDB code 2REB)12 is shown in continuous lines and form 2 is shown in broken lines. The form 1 and 2 structures are superimposed on the basis of the C^a atoms of the core domains of the monomer on the left. The difference in the helical transformation in forms 1 and 2 is evident from the poor overlap of the monomer on the right. Residues 6 and 33 are labeled to indicate the boundaries of the N-terminal domain. b, Close-up view of a in the region of the monomer-monomer interface. Notice that the orientation of the N-terminal domain of the left monomer is different in the form 1 and form 2 structures, according to the position of the neighboring subunit. The orientation of the N-terminal domain is adjusted to accommodate changes in helical pitch, while preserving atomic interactions at the monomer-monomer interface. This is observed also in the form 3 and form 4 structures, though shown here only for the form 1 and form 2 structures.

The above figure is reprinted by permission from Elsevier: J Mol Biol (2004, 342, 1471-1485) copyright 2004.