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

Protein Science : a Publication of the Protein Society
D S GarrettA M Gronenborn

Abstract

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 1H-15N correlation spectroscopy. The active site His 189 is phosphorylated at the Nepsilon2 position and has a pKa 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 Ndelta1-H tautomer, and its Nepsilon2 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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Citations

Sep 27, 2012·Journal of Biomolecular NMR·Francois-Xavier TheilletPhilipp Selenko
Jun 22, 1999·Chemistry & Biology·M C Pirrung
Sep 30, 2016·The Journal of Physical Chemistry. B·Abhijnan ChattopadhyayJunji Iwahara
Sep 1, 2012·Protein Science : a Publication of the Protein Society·Young-Joo Yun, Jeong-Yong Suh
Feb 14, 2002·Archives of Biochemistry and Biophysics·Ann Ginsburg, Alan Peterkofsky
Dec 12, 2000·The Journal of Organic Chemistry·M C PirrungV S Rana
Dec 26, 2001·Chemical Reviews·L N Johnson, R J Lewis
Jul 9, 2002·Biomacromolecules·Xin ChenFritz Vollrath

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