大肠杆菌磷酸烯醇丙酮酸：糖磷酸转移酶系统中酶I N端结构域磷酸化活性位点组氨酸的互变异构状态和pKa值
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.
作者信息
Garrett D S, Seok Y J, Peterkofsky A, Clore G M, Gronenborn A M
机构信息
Laboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, Maryland 20892-0520, USA.
出版信息
Protein Sci. 1998 Mar;7(3):789-93. doi: 10.1002/pro.5560070329.
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.
摘要
利用一键和远程1H-15N相关光谱法对大肠杆菌磷酸烯醇丙酮酸：糖磷酸转移酶系统中酶I的N端结构域的磷酸化形式进行了研究。活性位点His 189在Nε2位置被磷酸化，其pKa为7.3，比未磷酸化的His 189高一个pH单位。由于未磷酸化的His 189的中性形式处于Nδ1-H互变异构体中，其Nε2原子无法接触溶剂，并接受来自Thr 168羟基的氢键，His 189的质子化和磷酸化都必须伴随着His 189侧链构象的变化，具体来说，从未磷酸化状态下g+构象体中的χ(2)角变为磷酸化状态下的g-构象体。
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