Open AccessThe 2.8-Å structure of rat liver F 1 -ATPase: Configuration of a critical intermediate in ATP synthesis/hydrolysis
Author(s) -
M.A. Bianchet,
Joanne Hullihen,
Pedersen Pl,
L. Mario Amzel
Publication year - 1998
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.95.19.11065
Subject(s) - nucleotide , atp synthase , atp hydrolysis , atpase , enzyme , biochemistry , chemistry , carbamoyl phosphate synthetase , stereochemistry , atp synthase gamma subunit , reaction intermediate , catalysis , gene
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.