The epsilon subunit of bacterial and chloroplast F(1)F(0) ATPases. Structure, arrangement, and role of the epsilon subunit in energy coupling within the complex.
Recent studies show that the epsilon subunit of bacterial and chloroplast F(1)F(0) ATPases is a component of the central stalk that links the F(1) and F(0) parts. This subunit interacts with alpha, beta and gamma subunits of F(1) and the c subunit ring of F(0). Along with the gamma subunit, epsilon is a part of the rotor that couples events at the three catalytic sites sequentially with proton translocation through the F(0) part. Structural data on the epsilon subunit when separated from the complex and in situ are reviewed, and the functioning of this polypeptide in coupling within the ATP synthase is considered.
Capaldi
R A
RA
Institute of Molecular Biology, University of Oregon, Eugene, OR 97403, USA.
Schulenberg
B
B
D025181:ATP Synthetase Complexes; D000251:Adenosine Triphosphatases / Q000378:metabolism; D001426:Bacterial Proteins / Q000737:chemistry; D001665:Binding Sites; D002736:Chloroplasts / Q000201:enzymology*; D004926:Escherichia coli / Q000201:enzymology*; D008958:Models, Molecular; D009097:Multienzyme Complexes / Q000737:chemistry; D017856:Phosphotransferases (Phosphate Group Acceptor) / Q000737:chemistry; D010940:Plant Proteins / Q000737:chemistry; D006180:Proton-Translocating ATPases / Q000737:chemistry*
D001426:Bacterial Proteins; D009097:Multienzyme Complexes; D010940:Plant Proteins; D025181:ATP Synthetase Complexes; D017856:Phosphotransferases (Phosphate Group Acceptor); D000251:Adenosine Triphosphatases; D006180:Proton-Translocating ATPases