Quaternary structure of ATP synthases: Symmetry and asymmetry in the F1 moiety

Research output: Contribution to journalArticle

Abstract

It has been proposed that during ATP synthesis/hydrolysis F1 ATPases experience a complex pattern of nucleotide binding and release during the catalytic cycle (binding change mechanism). This type of mechanism has implications that can be correlated with the structure of the enzyme. F1-ATPases (stoichiometry α3β3γδε) are essentially a symmetrical trimer of pairs of the major subunits (α and β); the minor subunits (γ, δ and ε) are in single copies and interact with the trimer in an asymmetrical fashion. The asymmetry introduced by the minor subunits has important structural and functional consequences: (1) it introduces differences between the potentially equivalent binding and catalytic sites in the major subunits, (2) it restricts the ways in which a binding change mechanism can occur, and (3) it governs the way in which the F1 interacts with the (asymmetrical) F0 sector.

Original languageEnglish (US)
Pages (from-to)429-433
Number of pages5
JournalJournal of Bioenergetics and Biomembranes
Volume24
Issue number5
DOIs
StatePublished - Oct 1992

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Proton-Translocating ATPases
Adenosine Triphosphate
Catalytic Domain
Hydrolysis
Nucleotides
Binding Sites
Enzymes

ASJC Scopus subject areas

  • Physiology
  • Cell Biology

Cite this

Quaternary structure of ATP synthases : Symmetry and asymmetry in the F1 moiety. / Amzel, Mario L; Bianchet, Mario Antonio; Pedersen, Peter L.

In: Journal of Bioenergetics and Biomembranes, Vol. 24, No. 5, 10.1992, p. 429-433.

Research output: Contribution to journalArticle

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