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Titolo:
THE F-0 COMPLEX OF THE ESCHERICHIA-COLI ATP SYNTHASE - INVESTIGATION BY ELECTRON SPECTROSCOPIC IMAGING AND IMMUNOELECTRON MICROSCOPY
Autore:
BIRKENHAGER R; HOPPERT M; DECKERSHEBESTREIT G; MAYER F; ALTENDORF K;
Indirizzi:
UNIV OSNABRUCK,FACHBEREICH BIOL CHEM,ARBEITSGRP MIKROBIOL D-49069 OSNABRUCK GERMANY UNIV OSNABRUCK,FACHBEREICH BIOL CHEM,ARBEITSGRP MIKROBIOL D-49069 OSNABRUCK GERMANY UNIV GOTTINGEN,INST MIKROBIOL GOTTINGEN GERMANY
Titolo Testata:
European journal of biochemistry
fascicolo: 1, volume: 230, anno: 1995,
pagine: 58 - 67
SICI:
0014-2956(1995)230:1<58:TFCOTE>2.0.ZU;2-T
Fonte:
ISI
Lingua:
ENG
Soggetto:
PROTON-TRANSLOCATING ATPASE; B-SUBUNIT; H+-ATPASE; QUATERNARY STRUCTURE; F0 COMPLEX; CRYOELECTRON MICROSCOPY; TRANSMEMBRANE TOPOLOGY; THERMOPHILIC BACTERIUM; MEMBRANE-PROTEIN; UNC OPERON;
Keywords:
ELECTRON SPECTROSCOPIC IMAGING; IMMUNOELECTRON MICROSCOPY; F0F1 ATP SYNTHASE; F-0 COMPLEX; ESCHERICHIA COLI;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
74
Recensione:
Indirizzi per estratti:
Citazione:
R. Birkenhager et al., "THE F-0 COMPLEX OF THE ESCHERICHIA-COLI ATP SYNTHASE - INVESTIGATION BY ELECTRON SPECTROSCOPIC IMAGING AND IMMUNOELECTRON MICROSCOPY", European journal of biochemistry, 230(1), 1995, pp. 58-67

Abstract

Cholate-solubilized F-0 complexes of the ATP synthase (F0F1) from Escherichia coli were studied by application of conventional transmissionelectron microscopy and electron spectroscopic imaging (ESI) of negatively stained samples. Using the ESI mode, the structural organizationof the F-0 complex (diameter of 7.5 +/- 0.5 nm) could be observed in more detail and defined projections could be distinguished. ProjectionA appears as a deltoid-like structure with bilateral symmetry. Projection B has an overall trapezoidal shape with some similarity in shape to the letter W. Applying the ESI mode to the ac complex dissolved in cholate-containing buffer, an elongated structure consisting of two intensity maxima could be observed. Simulations with models of the F-0 and the ne complex revealed that the projections observed can be obtained by tilting and rotating a model in which subunit a and the two copies of subunit b are located outside the subunit c oligomer. This view of structural organization was supported by results obtained with F-0 complexes decorated with monoclonal antibodies against subunits a, b or c.

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Documento generato il 30/09/20 alle ore 06:05:48