HPr（细菌中的一种关键调节蛋白）中丝氨酸-46的磷酸化导致其溶液结构的稳定。
Phosphorylation of serine-46 in HPr, a key regulatory protein in bacteria, results in stabilization of its solution structure.
作者信息
Pullen K, Rajagopal P, Branchini B R, Huffine M E, Reizer J, Saier M H, Scholtz J M, Klevit R E
机构信息
Department of Biochemistry, University of Washington, Seattle 98195-7742, USA.
出版信息
Protein Sci. 1995 Dec;4(12):2478-86. doi: 10.1002/pro.5560041204.
Abstract
The serine-phosphorylated form of histidine-containing protein (HPr), a component of the phosphoenolpyruvate:sugar phosphotransferase system from Bacillus subtilis, has been characterized by NMR spectroscopy and solvent denaturation studies. The results indicate that phosphorylation of Ser 46, the N-cap of alpha-helix-B, does not cause a conformational change but rather stabilizes the helix. Amide proton exchange rates in helix-B are decreased and phosphorylation stabilizes the protein to solvent and thermal denaturation, with a delta delta G of 0.7-0.8 kcal mol-1. A mutant in which Ser 46 is replaced by aspartic acid shows a similar stabilization, indicating that an electrostatic interaction between the negatively charged groups and the helix macrodipole contributes significantly to the stabilization.
摘要
来自枯草芽孢杆菌的磷酸烯醇丙酮酸
糖磷酸转移酶系统的一个组分——含组氨酸蛋白（HPr）的丝氨酸磷酸化形式，已通过核磁共振光谱和溶剂变性研究进行了表征。结果表明，α-螺旋-B的N端帽Ser 46的磷酸化不会引起构象变化，反而会稳定该螺旋。螺旋-B中的酰胺质子交换速率降低，磷酸化使蛋白质对溶剂和热变性更稳定，ΔΔG为0.7 - 0.8千卡/摩尔。Ser 46被天冬氨酸取代的突变体表现出类似的稳定性，表明带负电荷的基团与螺旋大偶极之间的静电相互作用对稳定性有显著贡献。
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