The 2.8-Å structure of rat liver F1-ATPase: Configuration of a critical intermediate in ATP synthesis/hydrolysis

Mario A. Bianchet, Joanne Hullihen, Peter L. Pedersen, L. Mario Amzel

Research output: Contribution to journalArticlepeer-review

Abstract

During mitochondrial ATP synthesis, F1-ATPase - the portion of the ATP synthase that contains the catalytic and regulatory nucleotide binding sites - undergoes a series of concerted conformational changes that couple proton translocation to the synthesis of the high levels of ATP required for cellular function. In the structure of the rat liver F1-ATPase, determined to 2.8-Å resolution in the presence of physiological concentrations of nucleotides, all three β subunits contain bound nucleotide and adopt similar conformations. This structure provides the missing configuration of F1 necessary to define all intermediates in the reaction pathway. Incorporation of this structure suggests a mechanism of ATP synthesis/hydrolysis in which configurations of the enzyme with three bound nucleotides play an essential role.

Original languageEnglish (US)
Pages (from-to)11065-11070
Number of pages6
JournalProceedings of the National Academy of Sciences of the United States of America
Volume95
Issue number19
DOIs
StatePublished - Sep 15 1998

Keywords

  • ATP synthase
  • FF-ATPase
  • Mitochondria
  • Oxidative phosphorylation
  • X-ray diffraction

ASJC Scopus subject areas

  • General

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