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2
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4
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10
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Van der waals surfaces in molecular modeling: implementation with real-time computer graphics.分子建模中的范德华表面：实时计算机图形学的实现。
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Crystal structure of the catalytic subunit of cAMP-dependent protein kinase complexed with MgATP and peptide inhibitor.与MgATP和肽抑制剂复合的环磷酸腺苷依赖性蛋白激酶催化亚基的晶体结构。
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4
Mapping of the binding interfaces of the proteins of the bacterial phosphotransferase system, HPr and IIAglc.细菌磷酸转移酶系统中蛋白质HPr和IIAglc的结合界面图谱绘制
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5
The structures of native phosphorylated chicken cystatin and of a recombinant unphosphorylated variant in solution.天然磷酸化鸡半胱氨酸蛋白酶抑制剂及溶液中重组非磷酸化变体的结构。
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Phosphoenolpyruvate:carbohydrate phosphotransferase systems of bacteria.细菌的磷酸烯醇丙酮酸：碳水化合物磷酸转移酶系统
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Proteins. 1993 Sep;17(1):75-86. doi: 10.1002/prot.340170110.
8
Loss of protein kinase-catalyzed phosphorylation of HPr, a phosphocarrier protein of the phosphotransferase system, by mutation of the ptsH gene confers catabolite repression resistance to several catabolic genes of Bacillus subtilis.ptsH基因突变导致磷酸转移酶系统的磷酸载体蛋白HPr失去蛋白激酶催化的磷酸化作用，这使得枯草芽孢杆菌的几个分解代谢基因具有抗分解代谢物阻遏的特性。
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9
Inhibition of the phosphoenolpyruvate:lactose phosphotransferase system and activation of a cytoplasmic sugar-phosphate phosphatase in Lactococcus lactis by ATP-dependent metabolite-activated phosphorylation of serine 46 in the phosphocarrier protein HPr.通过磷酸载体蛋白HPr中丝氨酸46的ATP依赖性代谢物激活磷酸化作用，抑制乳酸乳球菌中的磷酸烯醇丙酮酸：乳糖磷酸转移酶系统并激活细胞质糖磷酸磷酸酶。
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10
The crystal structure of succinyl-CoA synthetase from Escherichia coli at 2.5-A resolution.大肠杆菌琥珀酰辅酶A合成酶在2.5埃分辨率下的晶体结构。
J Biol Chem. 1994 Apr 8;269(14):10883-90. doi: 10.2210/pdb1scu/pdb.

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.

DOI:10.1002/pro.5560041204
PMID:8580838
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC2143046/
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。