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Titolo:
Structural interpretations of F-0 rotary function in the Escherichia coli F1F0 ATP synthase
Autore:
Fillingame, RH; Jiang, W; Dmitriev, OY; Jones, PC;
Indirizzi:
Univ Wisconsin, Sch Med, Dept Biomol Chem, Madison, WI 53706 USA Univ Wisconsin Madison WI USA 53706 pt Biomol Chem, Madison, WI 53706 USA
Titolo Testata:
BIOCHIMICA ET BIOPHYSICA ACTA-BIOENERGETICS
fascicolo: 2-3, volume: 1458, anno: 2000,
pagine: 387 - 403
SICI:
0005-2728(20000531)1458:2-3<387:SIOFRF>2.0.ZU;2-7
Fonte:
ISI
Lingua:
ENG
Soggetto:
SUBUNIT-C; PROPIONIGENIUM-MODESTUM; H+-ATPASE; SUPPRESSOR MUTATIONS; CROSS-LINKING; PROTEOLIPID SUBUNIT; CRYSTAL-STRUCTURE; MEMBRANE DOMAIN; EPSILON-SUBUNIT; MOLECULAR-BASIS;
Keywords:
adenosine triphosphate synthase; proton transport; rotary motor; subunit c; F-0 structure;
Tipo documento:
Review
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
78
Recensione:
Indirizzi per estratti:
Indirizzo: Fillingame, RH Univ Wisconsin, Sch Med, Dept Biomol Chem, 1300 Univ Ave, Madison, WI 53706 USA Univ Wisconsin 1300 Univ Ave Madison WI USA 53706 53706 USA
Citazione:
R.H. Fillingame et al., "Structural interpretations of F-0 rotary function in the Escherichia coli F1F0 ATP synthase", BBA-BIOENER, 1458(2-3), 2000, pp. 387-403

Abstract

F1F0 ATP synthases are known to synthesize ATP by rotary catalysis in the Fl sector of the enzyme. Proton translocation through the F-0 membrane sector is now proposed to drive rotation of an oligomer of c subunits, which inturn drives rotation of subunit gamma in F-1. The primary emphasis of thisreview will be on recent work from our laboratory on the structural organization of F-0, which proves to be consistent with the concept of a c(12) oligomeric rotor. From the NMR structure of subunit c and cross-linking studies, we call now suggest a detailed model for the organization of the c(12) oligomer in F-0 and some of the transmembrane interactions with subunits a and b. The structural model indicates that the H+-carrying carboxyl of subunit c is located between subunits of the c(12) oligomer and that two c subunits pack in a front-to-back manner to form the proton (cation) binding site. The proton carrying Asp61 side chain is occluded between subunits and access to it, for protonation and deprotonation via alternate entrance and exit half-channels, requires a swiveled opening of the packed c subunits and stepwise association with different transmembrane helices of subunit a. We suggest how some of the structural information can be incorporated into models of rotary movement of the c(12) oligomer during coupled synthesis of ATP in the Fl portion of the molecule. (C) 2000 Elsevier Science B,V. All rights reserved.

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Documento generato il 21/01/20 alle ore 07:01:28