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Titolo:
Structure-function relationships of A-, F- and V-ATPases
Autore:
Gruber, G; Wieczorek, H; Harvey, WR; Muller, V;
Indirizzi:
Univ Saarland, FR Biophys 2 5, D-66421 Homburg, Germany Univ Saarland Homburg Germany D-66421 phys 2 5, D-66421 Homburg, Germany Univ Osnabruck, Dept Biol, D-49069 Osnabruck, Germany Univ Osnabruck Osnabruck Germany D-49069 iol, D-49069 Osnabruck, Germany Univ Florida, Whitney Lab, St Augustine, FL 32080 USA Univ Florida St Augustine FL USA 32080 ey Lab, St Augustine, FL 32080 USA Univ Munich, Lehrstuhl Mikrobiol, D-80638 Munich, Germany Univ Munich Munich Germany D-80638 hl Mikrobiol, D-80638 Munich, Germany
Titolo Testata:
JOURNAL OF EXPERIMENTAL BIOLOGY
fascicolo: 15, volume: 204, anno: 2001,
pagine: 2597 - 2605
SICI:
0022-0949(200108)204:15<2597:SROAFA>2.0.ZU;2-5
Fonte:
ISI
Lingua:
ENG
Soggetto:
COLI ATP SYNTHASE; MANDUCA-SEXTA MIDGUT; VACUOLAR H+-ATPASE; CLATHRIN-COATED VESICLE; C-SUBUNIT OLIGOMER; ESCHERICHIA-COLI; ELECTRON-MICROSCOPY; EPSILON-SUBUNIT; GAMMA-SUBUNIT; DELTA-SUBUNIT;
Keywords:
A(1)A(o)-ATPase; archaea-type ATPase; F1Fo-ATPase; H+ translocating vacuolar-type ATPase; V-1-ATPase; small-angle X-ray scattering; Escherichia coli; Manduca sexta; Methanosarcina mazei;
Tipo documento:
Review
Natura:
Periodico
Settore Disciplinare:
Agriculture,Biology & Environmental Sciences
Life Sciences
Citazioni:
80
Recensione:
Indirizzi per estratti:
Indirizzo: Gruber, G Univ Saarland, FR Biophys 2 5, D-66421 Homburg, Germany Univ Saarland Homburg Germany D-66421 D-66421 Homburg, Germany
Citazione:
G. Gruber et al., "Structure-function relationships of A-, F- and V-ATPases", J EXP BIOL, 204(15), 2001, pp. 2597-2605

Abstract

Ion-translocating ATPases, such as the F1Fo-, V1Vo- and archaeal A(1)A(o) enzymes, are essential cellular energy converters which transduce the chemical energy of ATP hydrolysis into transmembrane ionic electrochemical potential differences. Based on subunit composition and primary structures of the subunits, these types of ATPases are related through evolution; however, they differ with respect to function. Recent work has focused on the three-dimensional structural relationships of the major, nucleotide-binding subunits A and B of the A(1)/V-1-ATPases and the corresponding beta and alpha subunits of the F-1-ATPase, and the location of the coupling subunits within the stalk that provide the physical linkage between the regions of ATP hydrolysis and ion transduction. This review focuses on the structural homologies and diversities of A(1)-, F-1- and V-1-ATPases, in particular on significant differences between the stalk regions of these families of enzymes.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 09/07/20 alle ore 20:51:00