Coupling between catalytic sites and the proton channel in F1F0-type ATPases.
F1F0-type ATPases catalyse both ATP-driven proton translocation and proton-gradient-driven ATP synthesis. Recent cryoelectronmicroscopy and low-resolution X-ray studies provide a first glimpse at the structure of this complicated membrane-bound enzyme. The F1 part is roughly globular and linked to the membrane-intercalated F0 part by a narrow stalk domain, which contains the gamma-, delta- and epsilon-subunits along with domains of the b-subunit of the F0 part. Here, we review evidence that conformational and positional changes in the gamma- and epsilon-subunits provide the coupling between catalytic sites and proton translocation within the F1F0 complex.
Capaldi
R A
RA
Institute of Molecular Biology, University of Oregon, Eugene 97403.
Aggeler
R
R
Turina
P
P
Wilkens
S
S
D001665:Binding Sites; D002384:Catalysis; D009711:Nucleotides / Q000378:metabolism; D011487:Protein Conformation; D006180:Proton-Translocating ATPases / Q000737:chemistry* / Q000378:metabolism
D009711:Nucleotides; D006180:Proton-Translocating ATPases