Identification of phosphate binding residues of Escherichia coli ATP synthase.
Four positively-charged residues, namely betaLys-155, betaArg-182, betaArg-246, and alphaArg-376 have been identified as Pi binding residues in Escherichia coli ATP synthase. They form a triangular Pi binding site in catalytic site betaE where substrate Pi initially binds for ATP synthesis in oxidative phosphorylation. Positive electrostatic charge in the vicinity of betaArg-246 is shown to be one important component of Pi binding.
Ahmad
Zulfiqar
Z
Department of Biochemistry and Biophysics, University of Rochester Medical Center, Rochester, New York, USA.
Senior
Alan E
AE
D000596:Amino Acids; D001665:Binding Sites; D029968:Escherichia coli Proteins / Q000378:metabolism*; D025261:Mitochondrial Proton-Translocating ATPases / Q000378:metabolism*; D010085:Oxidative Phosphorylation; D010710:Phosphates / Q000378:metabolism*
D000596:Amino Acids; D029968:Escherichia coli Proteins; D010710:Phosphates; D025261:Mitochondrial Proton-Translocating ATPases