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Titolo:
STRUCTURAL FEATURES OF THE EPSILON-SUBUNIT OF THE ESCHERICHIA-COLI ATP SYNTHASE DETERMINED BY NMR-SPECTROSCOPY
Autore:
WILKENS S; DAHLQUIST FW; MCINTOSH LP; DONALDSON LW; CAPALDI RA;
Indirizzi:
UNIV OREGON,INST MOLEC BIOL EUGENE OR 97401 UNIV OREGON,INST MOLEC BIOL EUGENE OR 97401 UNIV BRITISH COLUMBIA,DEPT BIOCHEM & MOLEC BIOL VANCOUVER BC V6T 1Z3 CANADA UNIV BRITISH COLUMBIA,DEPT CHEM VANCOUVER BC V6T 1Z3 CANADA
Titolo Testata:
Nature structural biology
fascicolo: 11, volume: 2, anno: 1995,
pagine: 961 - 967
SICI:
1072-8368(1995)2:11<961:SFOTEO>2.0.ZU;2-6
Fonte:
ISI
Lingua:
ENG
Soggetto:
TRANSLOCATING ADENOSINE-TRIPHOSPHATASE; AMINO-ACID-SEQUENCE; H+-ATPASE; CRYOELECTRON MICROSCOPY; PROTEINS; PROTON; F1; NUCLEOTIDE; RESOLUTION; EXPRESSION;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
43
Recensione:
Indirizzi per estratti:
Citazione:
S. Wilkens et al., "STRUCTURAL FEATURES OF THE EPSILON-SUBUNIT OF THE ESCHERICHIA-COLI ATP SYNTHASE DETERMINED BY NMR-SPECTROSCOPY", Nature structural biology, 2(11), 1995, pp. 961-967

Abstract

The tertiary fold of the epsilon subunit of the Escherichia coli F1F0ATPsynthase (ECF(1)F(0)) has been determined by two- and three-dimensional heteronuclear (C-13, N-15) NMR spectroscopy. The epsilon subunitexhibits a distinct two domain structure, with the N-terminal 84 residues of the protein forming a 10-stranded beta-structure, and with theC-terminal 48 amino acids arranged as two alpha-helices running antiparallel to one another (two helix hairpin). The beta-domain folds as abeta-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 ofthe open side of the beta-sandwich to the c subunits of the membrane-embedded F-0 part.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 06/07/20 alle ore 05:51:48