ABC (ATP-binding cassette) transporters and helicases are large superfamili
es of seemingly unrelated proteins, whose functions depend on the energy pr
ovided by ATP hydrolysis. Comparison of the 3D structures of their nucleoti
de-binding domains reveals that, besides two well-characterized ATP-binding
signatures, the folds of their nucleotide-binding sites are similar. Furth
ermore, there are striking similarities in the positioning of residues thou
ght to be important for ATP binding or hydrolysis. Interestingly, structure
s have recently been obtained for two ABC proteins that are not involved in
transport activities, but that have a function related to DNA modification
. These ABC proteins, which contain a nucleotide-binding site akin to those
of typical ABC transporters, might constitute the missing link between the
two superfamilies.