Subunit organization and structure in the F0 sector of Escherichia coli F1F0 ATP synthase

R. H. Fillingame, P. C. Jones, W. Jiang, Francis Valiyaveetil, O. Y. Dmitriev

Research output: Contribution to journalArticle

52 Citations (Scopus)

Abstract

In this review, we summarize recent work from our laboratory which establishes the topology and nearest neighbor organization of subunits in the F0 sector of the H+ transporting ATP synthase of Escherichia coli. The E. coli F0 sector is composed of three subunits in an a1b2c12 stoichiometric ratio. Crosslinking experiments with genetically introduced Cys establish a ring-like organization of the 12 c subunits with subunits a and b lying to the outside of the ring. The results are interpreted using an atomic resolution structural model of monomeric subunit c in a chloroform- methanol-water (4:4:1, v/v/v) solution, derived by heteronuclear NMR (M.E. Girvin, F. Abildgaard, V. Rastogi, J. Markley, R.H. Fillingame, in press). The crosslinking results validate many predictions of the structural model and confirm a front-to-back-type packing of two subunit c into a functional dimer, as was first predicted from genetic studies. Aspartyl-61, the proton translocating residue, lies at the center of the four transmembrane helices of the functional dimer, rather than at the periphery of the subunit c ring. Subunit a is shown to fold with five transmembrane helices, and a functionally important interaction of transmembrane helix-4 with transmembrane helix-2 of subunit c is established. The single transmembrane helices of the two subunit b dimerize in the membrane. The structure of the transmembrane segment of subunit b is predicted from the NMR structure of the monomeric peptide.

Original languageEnglish (US)
Pages (from-to)135-142
Number of pages8
JournalBiochimica et Biophysica Acta - Bioenergetics
Volume1365
Issue number1-2
DOIs
StatePublished - Jun 10 1998
Externally publishedYes

Fingerprint

Structural Models
Dimers
Crosslinking
Escherichia coli
Nuclear magnetic resonance
Biomolecular Nuclear Magnetic Resonance
Proton-Translocating ATPases
Chloroform
Methanol
Protons
Topology
Membranes
Peptides
Water
Experiments
F1F0-ATP synthase

Keywords

  • ATP synthase
  • Crosslinking
  • F structure
  • NMR
  • Proton translocation
  • Subunit c

ASJC Scopus subject areas

  • Biophysics

Cite this

Subunit organization and structure in the F0 sector of Escherichia coli F1F0 ATP synthase. / Fillingame, R. H.; Jones, P. C.; Jiang, W.; Valiyaveetil, Francis; Dmitriev, O. Y.

In: Biochimica et Biophysica Acta - Bioenergetics, Vol. 1365, No. 1-2, 10.06.1998, p. 135-142.

Research output: Contribution to journalArticle

Fillingame, R. H. ; Jones, P. C. ; Jiang, W. ; Valiyaveetil, Francis ; Dmitriev, O. Y. / Subunit organization and structure in the F0 sector of Escherichia coli F1F0 ATP synthase. In: Biochimica et Biophysica Acta - Bioenergetics. 1998 ; Vol. 1365, No. 1-2. pp. 135-142.
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