GabR is a transcription factor from Bacillus subtilis regulating the metabolism of γ-aminobutyric acid (GABA), an important source of nitrogen and carbon in bacteria, and also the chief inhibitory neurotransmitter in the mammalian central nervous system. GabR is known to interact simultaneously with two DNA binding sites and structural data suggests that GabR is dimeric. The crystal structure of GabR reveals that the two DNA binding domains are on opposite sides of the GabR dimer and not in a position that is compatible with the spacing between the binding sites on a linear double stranded DNA. Hence, it has been postulated that the protein must undergo a conformational change in order to bind DNA. In addition, two conflicting models suggest either one or two GabR dimers bind per DNA strand. We have, using SAXS, determined the solution shape of GabR bound and unbound with DNA, which demonstrates that the shape of GabR in solution is consistent with the dimeric crystal structure and that one dimer of GabR binds to DNA. The maximum dimension of the GabR/DNA complex is smaller than for DNA alone, revealing that on GabR binding, the DNA bends significantly with a curvature that is equivalent to chromatin-bound DNA. This curvature facilitates the simultaneous interaction of the GabR dimer with both binding sites on the DNA and indicates that a major conformational change in the protein is not required for this interaction as previously postulated.