ATP synthase: structure-function relationships

Philip J. Thomas, Mario Antonio Bianchet, David N. Garboczi, Joanne Hullihen, Mario L Amzel, Peter L Pedersen

Research output: Contribution to journalArticle

Abstract

Recent work has focused on obtaining a better understanding of the three-dimensional structural relationships between the α and β subunits of the F1 moiety and the location of nucleotide binding domains within these subunits. Four types of approach are currently being pursued: X-ray crystallographic, chemical, molecular biological and biochemical. Here we briefly review some of the major conclusions of these studies, and point out some of the problems that must be resolved before an adequate model that relates structure to function in the ATP synthase molecule can be formulated.

Original languageEnglish (US)
Pages (from-to)228-231
Number of pages4
JournalBiochimica et Biophysica Acta - Bioenergetics
Volume1101
Issue number2
DOIs
StatePublished - Jan 1 1992

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Nucleotides
Adenosine Triphosphate
X-Rays
X rays
Molecules

Keywords

  • ATP synthase
  • ATP synthesis
  • ATPase, F-

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Cell Biology

Cite this

ATP synthase : structure-function relationships. / Thomas, Philip J.; Bianchet, Mario Antonio; Garboczi, David N.; Hullihen, Joanne; Amzel, Mario L; Pedersen, Peter L.

In: Biochimica et Biophysica Acta - Bioenergetics, Vol. 1101, No. 2, 01.01.1992, p. 228-231.

Research output: Contribution to journalArticle

Thomas, Philip J. ; Bianchet, Mario Antonio ; Garboczi, David N. ; Hullihen, Joanne ; Amzel, Mario L ; Pedersen, Peter L. / ATP synthase : structure-function relationships. In: Biochimica et Biophysica Acta - Bioenergetics. 1992 ; Vol. 1101, No. 2. pp. 228-231.
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