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Protein Science, Vol 7, Issue 3 789-793, Copyright © 1998 by Cold Spring Harbor Laboratory Press

FOR THE RECORD

Tautomeric state and pK(a) of the phosphorylated active site histidine in the N-terminal domain of enzyme I of the Escherichia coli phosphoenolpyruvate:sugar phosphotransferase system

D. S. GARRETT, Y. J. SEOK, A. PETERKOFSKY, G. M. CLORE and A. M. GRONENBORN
Laboratory of Chemical Physics, Building 5, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, Maryland 20892-0520

The phosphorylated form of the N-terminal domain of enzyme I of the phosphoenolpyruvate:sugar phosphotransferase system of Escherichia coli has been investigated by one-bond and long-range (1)H-(15)N correlation spectroscopy. The active site His 189 is phosphorylated at the N{epsilon}2 position and has a pK(a) of 7.3, which is one pH unit higher than that of unphosphorylated His 189. Because the neutral form of unphosphorylated His 189 is in the N{delta}1-H tautomer, and its N{epsilon}2 atom is solvent inaccessible and accepts a hydrogen bond from the hydroxyl group of Thr 168, both protonation and phosphorylation of His 189 must be accompanied by a change in the side-chain conformation of His 189, specifically from a {chi}(2) angle in the g(+) conformer in the unphosphorylated state to the g(-) conformer in the phosphorylated state.
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