Data from: LRET-derived HADDOCK structural models describe the conformational heterogeneity required for processivity of the Mre11-Rad50 DNA damage repair complex

The Mre11-Rad50-Nbs1 protein complex is one of the first responders to DNA
double strand breaks. Studies have shown that the catalytic activities of
the evolutionarily conserved Mre11-Rad50 (MR) core complex depend on an
ATP-dependent global conformational change that takes the macromolecule
from an open, extended structure in the absence of ATP to a closed,
globular structure when ATP is bound. We have previously identified an
additional ‘partially open’ conformation using Luminescence Resonance
Energy Transfer (LRET) experiments. Here, a combination of LRET and the
molecular docking program HADDOCK was used to further investigate this
partially open state and identify three conformations of ATP-bound MR in
solution: closed, partially open, and open, which are in addition to the
extended, apo conformation. These models are supported with mutagenesis
and SAXS data that corroborate the presence of these three states and
suggest a mechanism for the processivity of the MR complex along the DNA.