Structural features of the epsilon subunit of the Escherichia coli ATP synthase determined by NMR spectroscopy.

TitleStructural features of the epsilon subunit of the Escherichia coli ATP synthase determined by NMR spectroscopy.
Publication TypeJournal Article
Year of Publication1995
AuthorsWilkens, S, Dahlquist, FW, McIntosh, LP, Donaldson, LW, Capaldi, RA
JournalNat Struct Biol
Volume2
Issue11
Pagination961-7
Date Published1995 Nov
ISSN1072-8368
KeywordsAmino Acid Sequence, Carbon Isotopes, Escherichia coli, Magnetic Resonance Spectroscopy, Models, Molecular, Molecular Sequence Data, Mutation, Nitrogen Isotopes, Protein Conformation, Protein Folding, Protein Structure, Secondary, Proton-Translocating ATPases
Abstract

The tertiary fold of the epsilon subunit of the Escherichia coli F1F0 ATPsynthase (ECF1F0) has been determined by two- and three-dimensional heteronuclear (13C, 15N) NMR spectroscopy. The epsilon subunit exhibits a distinct two domain structure, with the N-terminal 84 residues of the protein forming a 10-stranded beta-structure, and with the C-terminal 48 amino acids arranged as two alpha-helices running antiparallel to one another (two helix hairpin). The beta-domain folds as a beta-sandwich with a hydrophobic interior between the two layers of the sandwich. The C-terminal two-helix hairpin folds back to the N-terminal domain and interacts with one side of the beta-domain. The arrangement of the epsilon subunit in the intact F1F0 ATP synthase involves interaction of the two helix hairpin with the F1 part, and binding of the open side of the beta-sandwich to the c subunits of the membrane-embedded F0 part.

Alternate JournalNat. Struct. Biol.
Citation Key3247
PubMed ID7583669