Integration host factor (IHF) is a small heterodimeric protein that sp
ecifically binds to DNA and functions as an architectural factor in ma
ny cellular processes in prokaryotes. Here, we report the crystal stru
cture of IHF complexed with 35 bp of DNA. The DNA is wrapped around th
e protein and bent by >160 degrees, thus reversing the direction of th
e helix axis within a very short distance. Much of the bending occurs
at two large kinks where the base stacking is interrupted by intercala
tion of a proline residue. IHF contacts the DNA exclusively via the ph
osphodiester backbone and the minor groove and relies heavily on indir
ect readout to recognize its binding sequence. One such readout involv
es a six-base A tract, providing evidence for the importance of a narr
ow minor groove.