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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
JournalNature Structural Biology
Volume2
Pagination961-967
Date PublishedNov
Type of ArticleArticle
ISBN Number1072-8368
KeywordsAMINO-ACID-SEQUENCE, CRYOELECTRON MICROSCOPY, EXPRESSION, F1, H+-ATPASE, NUCLEOTIDE, PROTEINS, PROTON, RESOLUTION, TRANSLOCATING ADENOSINE-TRIPHOSPHATASE
Abstract

The tertiary fold of the epsilon subunit of the Escherichia coli F1F0 ATPsynthase (ECF(1)F(0)) has been determined by two- and three-dimensional heteronuclear (C-13, N-15) 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 F-1 part, and binding of the open side of the beta-sandwich to the c subunits of the membrane-embedded F-0 part.

URL<Go to ISI>://A1995TD55400013