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. Author manuscript; available in PMC: 2011 Dec 10.
Published in final edited form as: DNA Repair (Amst). 2010 Oct 28;9(12):1299–1306. doi: 10.1016/j.dnarep.2010.10.001

Figure 3.

Figure 3

The Mre11 dimer adopts different conformational states at a 2-ended Vs 1-ended DSB. (A) Crystal structures of Mre11 in complex with a 2-ended DSB (top) or a 1-ended DSB replication fork mimic (bottom) revealed Mre11 binds these DNA substrates as symmetric and asymmetric dimers respectively. (B) Cartoon of Mre11 bound to DNA substrates as in (A) with phosphodiesterase and capping domains colored blue and gray, respectively, as in Fig. 1B. Arrows highlight the Mre11 phosphodiesterase and DNA capping domain rotations required to move between 2-ended and 1-ended bound states. ATLD sites that reduce Nbs1 binding (N117S and W210C, green and yellow respectively) are mapped onto the surface and the dotted outline of the symmetric Mre11 dimer is overlaid on the asymmetric dimer to highlight rearrangements between the two states.