Crystal structure of the epsilon subunit of the proton-translocating ATP synthase from Escherichia coli.
Uhlin, U., Cox, G.B., Guss, J.M.(1997) Structure 5: 1219-1230
- PubMed: 9331422 
- DOI: https://doi.org/10.1016/s0969-2126(97)00272-4
- Primary Citation of Related Structures:  
1AQT - PubMed Abstract: 
Proton-translocating ATP synthases convert the energy generated from photosynthesis or respiration into ATP. These enzymes, termed F0F1-ATPases, are structurally highly conserved. In Escherichia coli, F0F1-ATPase consists of a membrane portion, F0, made up of three different polypeptides (a, b and c) and an F1 portion comprising five different polypeptides in the stoichiometry alpha 3 beta 3 gamma delta epsilon. The minor subunits gamma, delta and epsilon are required for the coupling of proton translocation with ATP synthesis; the epsilon subunit is in close contact with the alpha, beta, gamma and c subunits. The structure of the epsilon subunit provides clues to its essential role in this complex enzyme.
Organizational Affiliation: 
Department of Biochemistry, University of Sydney, NSW, Australia.