PMID:9331422

Citation	Uhlin, U, Cox, GB and Guss, JM (1997) Crystal structure of the epsilon subunit of the proton-translocating ATP synthase from Escherichia coli. Structure 5:1219-30
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.
Links	PubMed
Keywords	Amino Acid Sequence; Animals; Cattle; Conserved Sequence/genetics; Crystallography, X-Ray; Escherichia coli/enzymology; Hydrogen Bonding; Magnetic Resonance Spectroscopy; Mitochondria/enzymology; Models, Molecular; Molecular Sequence Data; Mutation/genetics; Protein Conformation; Protein Folding; Protein Structure, Secondary; Proton-Translocating ATPases/chemistry; Proton-Translocating ATPases/genetics; Protons; Sequence Alignment
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