Identification of alpha-subunit Lys201 and beta-subunit Lys155 at the ATP-binding sites in Escherichia coli F1-ATPase.
Binding of about 1 mol of adenosine triphosphopyridoxal to Escherichia coli F1-ATPase resulted in the nearly complete inactivation of the enzyme [(1987) J. Biol. Chem. 262, 7686-7692]. About two thirds of the label was bound to the alpha-subunit, and the rest to the beta-subunit. The present study revealed that Lys201 in the alpha-subunit and Lys155 in the glycine-rich region of the beta-subunit are the major sites labeled with this reagent. Thus, these two residues might be located close to the gamma-phosphate of the bound ATP.
D000255:Adenosine Triphosphate / Q000378:metabolism*; D000595:Amino Acid Sequence; D001665:Binding Sites; D002850:Chromatography, Gel; D004926:Escherichia coli / Q000201:enzymology*; D008239:Lysine; D046911:Macromolecular Substances; D010446:Peptide Fragments / Q000032:analysis; D006180:Proton-Translocating ATPases / Q000378:metabolism*
D046911:Macromolecular Substances; D010446:Peptide Fragments; D000255:Adenosine Triphosphate; D006180:Proton-Translocating ATPases; D008239:Lysine