Conformational changes in the gamma and epsilon subunits are integral to the functioning of the Escherichia coli H(+)-pumping ATPase (ECF1F0).
ATP synthesis and ATP hydrolysis by F1F0-type ATPases involve conformational changes transmitted from the catalytic site regions to the proton channel, a distance of more than 100 A. Our studies focus attention on the gamma and epsilon subunits that provide a part of the stalk region in the energy-coupling process within the complex. There are conformational changes in the gamma subunit, and translocations of the epsilon unit, linked to nucleotide-binding changes in catalytic sites, which might be expected to alter the interaction of this subunits with c subunits and, hence, be linked to proton translocation.
Capaldi
R A
RA
Institute of Molecular Biology, University of Oregon, Eugene 97403, USA.
Aggeler
R
R
Wilkens
S
S
D000255:Adenosine Triphosphate / Q000096:biosynthesis / Q000378:metabolism; D001665:Binding Sites; D002384:Catalysis; D004926:Escherichia coli / Q000201:enzymology* / Q000235:genetics; D015394:Molecular Structure; D017354:Point Mutation; D011487:Protein Conformation; D006180:Proton-Translocating ATPases / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*
D000255:Adenosine Triphosphate; D006180:Proton-Translocating ATPases