Gal repressosome assembly and repression of the gal operon in Escherichia c
oli occurs when two dimeric GalR proteins and the histone-like HU protein b
ind to cognate sites causing DNA looping. Structure-based genetic analysis
defined the GalR surfaces interacting to form a stacked, V-shaped, tetramer
ic structure. Stereochemical models of the four possible DNA loops compatib
le with the GalR tetramer configuration were constructed using the sequence
-dependent structural parameters of the interoperator DNA and conformation
changes caused by GalR and asymmetric HU binding. Evaluation of their DNA e
lastic energies gave unambiguous preference to a loop structure in which th
e two gal operators adopt an antiparallel orientation causing undertwisting
of DNA.