A) Analysis of the probability of coiled coil regions within B. subtilis SbcC, using programs from http://npsa-pbil.ibcp.fr. The position of the corresponding CXXC motif forming a Zn bridge in Rad50  is indicated. B) Analysis of the formation of α-helices in SbcC. C) Putative structure of SbcC, and putative binding of SbcD, according to data obtained for Rad50 protein [18, 56]. SbcC has the potential to form a dimer with another SbcC monomer via the Zn-bridge. It is interesting to note that in spite of their similarity, the SbcCD and Rad50/Mre11 complexes have a different arrangement in vitro .