Helix-turn-helix motif is one of the common motifs observed in DNA-bin
ding proteins. The motif interacts with DNA double helix and recognize
s specific base sequences. It is assumed that the helix - turn - helix
motif appears only once in seven prokaryotic transcriptional represso
rs of which 3-D structures have been determined by X-ray crystallograp
hic studies. These prokaryotic repressors consist of several alpha-hel
ices connected with turns. We report here that these repressors are de
composable into helix - turn - helix modules and their connectors. A m
odule is defined as a compact structural unit with consecutive amino a
cid residues in a globular protein. Each of the helix - turn - helix m
otifs in the seven proteins corresponds approximately to a single heli
x-turn-helix module consisting of approximately 13 amino acids. Identi
fication of modules of seven prokaryotic repressors and comparisons of
their tertiary structures led to the conclusion that three of these D
NA-binding proteins contain more than one helix - turn - helix module
with a structure similar to the helix-turn-helix motif. The difference
in module organization of these DNA-binding proteins paves the way fo
r further classification of the DNA-binding proteins with the helix-tu
rn-helix motif. The structural repertoire of these transcriptional reg
ulators was increased through different utilizations in the number of
helix - turn - helix and other modules. The difference in DNA base rec
ognition ability in these helix - turn - helix modules is ascribed to
a difference in size of a side chain at the fifth residue from Gly, on
the turn.