A common mechanism for ATP hydrolysis in ABC transporter and helicase superfamilies.
ABC (ATP-binding cassette) transporters and helicases are large superfamilies of seemingly unrelated proteins, whose functions depend on the energy provided by ATP hydrolysis. Comparison of the 3D structures of their nucleotide-binding domains reveals that, besides two well-characterized ATP-binding signatures, the folds of their nucleotide-binding sites are similar. Furthermore, there are striking similarities in the positioning of residues thought to be important for ATP binding or hydrolysis. Interestingly, structures 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.
Geourjon
C
C
Laboratoire de Bioinformatique et RMN structurales, UMR 5086 CNRS-Université Claude Bernard de Lyon, 7 Passage du Vercors, F-69367 Lyon Cedex 07, France.
Orelle
C
C
Steinfels
E
E
Blanchet
C
C
Deléage
G
G
Di Pietro
A
A
Jault
J M
JM
D018528:ATP-Binding Cassette Transporters / Q000737:chemistry* / Q000378:metabolism*; D000255:Adenosine Triphosphate / Q000378:metabolism*; D020816:Amino Acid Motifs; D001665:Binding Sites; D004265:DNA Helicases / Q000737:chemistry* / Q000378:metabolism*; D006868:Hydrolysis; D011487:Protein Conformation
D018528:ATP-Binding Cassette Transporters; D000255:Adenosine Triphosphate; D004265:DNA Helicases