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Titolo:
Quaternary structure of V-1 and F-1 ATPase: Significance of structural homologies and diversities
Autore:
Svergun, DI; Konrad, S; Huss, M; Koch, MHJ; Wieczorek, H; Altendorf, K; Volkov, VV; Gruber, G;
Indirizzi:
Univrmanybruck, Fachbereich Biol Chem, Abt Mikrobiol, D-49069 Osnabruck, Ge Univ Osnabruck Osnabruck Germany D-49069 ikrobiol, D-49069 Osnabruck, Ge Univermanyruck, Fachbereich Biol Chem, Abt Zoophysiol, D-49069 Osnabruck, G Univ Osnabruck Osnabruck Germany D-49069 oophysiol, D-49069 Osnabruck, G European Mol Biol Lab, Hamburg Outstn, D-22603 Hamburg, Germany European Mol Biol Lab Hamburg Germany D-22603 , D-22603 Hamburg, Germany Russian Acad Sci, Inst Crystallog, Moscow 117333, Russia Russian Acad SciMoscow Russia 117333 Crystallog, Moscow 117333, Russia
Titolo Testata:
BIOCHEMISTRY
fascicolo: 51, volume: 37, anno: 1998,
pagine: 17659 - 17663
SICI:
0006-2960(199812)37:51<17659:QSOVAF>2.0.ZU;2-5
Fonte:
ISI
Lingua:
ENG
Soggetto:
SMALL-ANGLE-SCATTERING; DIRECT SHAPE DETERMINATION; TOBACCO HORNWORM MIDGUT; VACUOLAR H+-ATPASE; V-ATPASE; SYNCHROTRON RADIATION; NEUROSPORA-CRASSA; KDA SUBUNIT; MEMBRANE; PURIFICATION;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
47
Recensione:
Indirizzi per estratti:
Indirizzo: Gruber, G Univrmanybruck, Fachbereich Biol Chem, Abt Mikrobiol, D-49069 Osnabruck, Ge Univ Osnabruck Osnabruck Germany D-49069 D-49069 Osnabruck, Ge
Citazione:
D.I. Svergun et al., "Quaternary structure of V-1 and F-1 ATPase: Significance of structural homologies and diversities", BIOCHEM, 37(51), 1998, pp. 17659-17663

Abstract

The V-1 ATPase from the tobacco hornworm Manduca sexta and the Escherichiacoli F-1 ATPase were characterized by small-angle X-ray scattering (SAXS). The radii of gyration (R-g) of the complexes were 6.2 +/- 0.1 and 4.7 +/- 0.02 nm, respectively. The shape of the M. sexta V-1 ATPase was determined ab initio from the scattering data showing six masses, presumed to be the Aand B subunits, arranged in an alternating manner about a 3-fold axis. A seventh mass with a length of about 11.0 nm extends perpendicularly to the center of the hexameric unit. This central mass is presumed to be the stalk that connects V-1 with the membrane domain (V-o) in the intact V1Vo-ATPase. In comparison, the shape of the F-1 ATPase from E. coli possesses a quasi-3-fold symmetry over the major part of the enzyme. The overall asymmetry ofthe structure is given by a stem, assumed to include the central stalk subunits. The features of the V-1 and F-1 ATPase reveal structural homologies and diversities of the key components of the complexes.

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Documento generato il 12/07/20 alle ore 08:47:47