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. 2014 Oct 27;33(23):2847–2859. doi: 10.15252/embj.201488889

Figure 2. Details of the Rad50NBD–Mre11HLH:DNA interface.

Figure 2

  1. Detailed view of the DNA interactions with the Rad50 NBD (orange) shown in ribbon representation with the contacting residues highlighted as sticks. DNA contacts involve interactions of the strand-loop-helix motif of the Rad50 dimer (residues K99, K108, K109, A111, A114, K115, and S118) with the sugar–phosphate backbone of the two DNA molecules (cyan and gray). The second DNA molecule, depicted in gray, belongs to the symmetry-related molecule and forms a quasi-continuous DNA strand in the crystal structure. Residues R94 and K95 are in close proximity of the DNA-binding region and evidently involved in DNA binding.
  2. Details of the DNA–protein contacts at the Rad50 coiled-coil region mediated by interactions of lysine residues K175, K178, and K182 with the DNA–phosphate backbone.
  3. Sequence alignment showing the conservation of residues involved in DNA binding.